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Biochemistry Research International
Biochemistry Research International / 2010 / Article
AbstractIntroductionMaterials and MethodsResultsDiscussionAcknowledgmentsReferencesCopyright
Lingyi Lynn Deng, Alice A. Alexander, Sijin Lei, John S. Anderson, "The Cell Wall Teichuronic Acid Synthetase (TUAS) Is an Enzyme Complex Located in the Cytoplasmic Membrane of Micrococcus luteus", Biochemistry Research International, vol. 2010, Article ID 395758, 8 pages, 2010. https://doi.org/10.1155/2010/395758
The Cell Wall Teichuronic Acid Synthetase (TUAS) Is an Enzyme Complex Located in the Cytoplasmic Membrane of Micrococcus luteus
Lingyi Lynn Deng,1,2,3 Alice A. Alexander,2 Sijin Lei,1,4 and John S. Anderson1
1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN 55108, USA
2Research Service, VA Boston Healthcare System, Boston, MA 02130, USA
3Department of Medicine, Boston University School of Medicine, 650 Albany Street, X-Rm808, Boston, MA 02118, USA
4St. Jude Medical, Inc., St. Paul, MN 55117, USA
Academic Editor: Robert J. Linhardt
Accepted18 Jan 2010
Published06 Apr 2010
The cell wall teichuronic acid (TUA) of Micrococcus luteus is a long-chain polysaccharide composed of disaccharide repeating units , which is covalently anchored to the peptidoglycan on the inner cell wall and extended to the outer surface of the cell envelope. An enzyme complex responsible for the TUA chain biosynthesis was purified and characterized. The 440 kDa enzyme complex, named teichuronic acid synthetase (TUAS), is an octomer composed of two kinds of glycosyltransferases, Glucosyltransferase, and ManNAcA-transferase, which is capable of catalyzing the transfer of disaccharide glycosyl residues containing both glucose and the -acetylmannosaminuronic acid residues. TUAS displays hydrophobic properties and is found primarily associated with the cytoplasmic membrane. The purified TUAS contains carotinoids and lipids. TUAS activity is diminished by phospholipase digestion. We propose that TUAS serves as a multitasking polysaccharide assembling station on the bacterial membrane.
Micrococcus luteus is a typical gram-positive bacterium. The cell wall teichuronic acid (TUA) is a long chain polysaccharide composed of almost a hundred disaccharide repeating units. TUA plays an important role in protecting the microbe and interacting with the host cells. TUA consists of D-glucose and N-acetyl-D-mannosaminuronic acid (ManNAcA) residues, in which the structural repeat unit is [→4)ß-D-ManNAcAp-(1→6) -D-Glcp -(1→ n [1, 2] (Figure 1). It is located on the cell surface and is covalently linked to peptidoglycan in M. luteus cell walls through a linker. Although experimental transfer of linkage oligosaccharide (or growing TUA chain) from carrier lipid to peptidoglycan remains to be demonstrated, the linkage region is found to be composed of a phosphate and an oligosaccharide as shown in Figures 1 and 6 [3, 4]. In vitro initial (de novo) synthesis of teichuronic acid by cytoplasmic membrane fragments requires uridine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc), uridine diphosphate N-acetyl-D-mannosaminuronic acid (UDP-ManNAcA), and UDP-glucose [3]. During biosynthesis, UDP-GlcNAc is the donor of the initial residue, which becomes the potentially reducing terminal residue of native teichuronic acid. However, wall-membrane preparations require only UDP-glucose and UDP-ManNAcA to effect elongation of teichuronic acid already present in the wall fragments [5]. Similarly, if exogenous soluble teichuronic acid is supplied as acceptor, UDP-glucose and UDP-ManNAcA are codependently required by detergent solubilized extracts of cytoplasmic membrane fragments to effect significant elongation of the acceptor teichuronic acid [6]. Transfer of glucosyl residues from UDP-glucose to teichuronic acid is catalyzed by glucosyltransferase and the addition of N-acetylmannosaminuronic acid residues is catalyzed by the ManNAcA-transferase (Figure 1). Very little is known about how these two enzymes are arranged and located, what other protein factors are also involved in the process of the polysaccharide biosynthesis, and how this extracellular polysaccharide is synthesized, elongated, and transported.
Chemical structure of teichuronic acid in the cell wall of Micrococcus luteus and proposed site of action for glucosyltransferase (indicated by arrow 1) and that for ManNAcA transferase (indicated by arrow 2). The linker contains an oligosaccharide with a GlcNAc residue at the reducing end and a phosphate.
Membrane preparations of Micrococcus luteus are easily prepared by lysozyme digestion and solubilization of the cell wall. Protoplasts are generated if the lysozyme treatment is done in osmotically stabilizing medium and membrane fragments or ghosts are produced in hypotonic medium. Because of the ease of cell wall removal, M. luteus constitutes an excellent model system for studying the structural organization of membrane components as well as investigation of membrane function [7]. The most extensively characterized enzyme of the membrane of this organism is the F1-ATPase which constitutes up to 10% of total membrane protein.
Little is known about the membrane placement of polymer synthesizing enzymes or how they participate in the vectorial process, in which a substrate produced in the cytoplasm is utilized for synthesis of an external polymer. To initiate an investigation of such vectorial relationships, we have examined the cytological localization of an enzyme involved in the biosynthesis of teichuronic acid in M. luteus, namely, the teichuronic acid synthetase.
In our early study of cell wall biosynthesis, cytoplasmic membrane fragments, solubilized with the detergents Thesit and CHAPS, were a source of glycosyltransferase. The enzyme was purified about 200-fold, and found to be a 440 kDa protein, which was responsible for TUA elongation. The purified native enzyme was a multisubunit protein consisting of subunits of two sizes (four copies of each); their molecular masses were determined to be 52.5 and 54 kDa. Since the radioactive assay is based on measuring the incorporation of [14C]glucose from UDP-[14C]glucose into TUA polymer, we tentatively classified this protein as a Glucosyltransferase [8]. In the current study, the same protein was further characterized by analyzing the physical and chemical properties as well as the subcellular locations. The additional biological function of this enzyme complex was discovered and a topological model is proposed.
2.1. Growth of Bacteria, Preparation, and Isolation of Cellular Fractions
Cultures of Micrococcus luteus (ATCC 4698) were grown at C in a vigorously shaken liquid culture medium containing peptone (10 g/liter) and NaCl (5 g/liter). The cells were usually harvested in the mid-log phase.
In general, the crude cell extract (bacterial lysate) was obtained by digesting the cell pellet with lysozyme, and then with DNase and RNase. The membrane fraction was obtained by centrifugation between 3,000 and 12,000 . The cytoplasmic membrane fragments were recovered from the supernatant by further centrifugation at 48,000 for l hour. The final pellet was washed several times and solubilized in a buffer containing detergents, Thesit, and CHAPS, with glycerol and magnesium ion to stabilize the solubilized enzyme [8].
To determine the TUAS activity in the different subcellular compartments, a specific experiment was conducted in which crude cell extract was prepared by physically grinding cells with alumina instead of lysozyme digestion [5]. Thus four fractions were obtained including (1) cytosol, (2) cytoplasmic membrane, (3) the cell wall, and (4) the culture supernatant or extracellular cell filtrate. The protein concentration in each fraction was standardized to 1 g/ml before the TUAS assay.
The cytosol fraction was prepared by filtering crude cell extract through two 0.22 mm Millipore nitrocellulose filters under vacuum.
The wall-membrane fraction was recovered by a slower speed centrifugation (3,000 to 12,000 ) of a crude extract. The wall-membrane fraction was loaded onto a sucrose step gradient consisting of equal volumes of 14, 16, and 17% sucrose and centrifuged at 18,000 rpm. The cell wall fraction was collected from the bottom of the gradient and the membrane fraction from the region of the junction between 14 and 16% sucrose layers and was further solubilized by the detengent Thesit (50 mg/ml) and CHAPS (0.5 mg/ml) [6].
The culture supernatant was precipitated by addition of ammonium sulfate to a concentration of 0.25 g/ml and collected by centrifugation at 12,000 for 25 minutes. The precipitate was resuspended and dialyzed against the same buffer. Extraneous ions were removed by passage of the sample through an ion retardation column (Bio-Rad).
2.2. Purification of the Enzyme Complex
The following steps were used to purify TUAS from detergent-solubilized extract or the membrane fraction: adsorbent column chromatography (Bio-Bead SM-2, flow through), anionic ion exchange chromatography (DEAE-cellulose column, eluted with 0.25 M NaCl), size exclusion chromatography (Bio-Gel P-300 column, exclusion/void volume), isoelectric precipitation (pH 5.5), ammonium sulfate fractionation (top layer), adsorbent column, and preparative gradient polyacrylamide gel electrophoresis [8].
2.3. Enzymatic Assays of TUAS
TUAS activity was determined by incubating 50 l of enzyme sample (liquid sample or gel slices) and 50 l of reaction mix at for 60 minutes. The complete reaction mixture contained 0.5–0.7 mM UDP-[14C]glucose (2 Ci/umol), 0.5–0.7 mM UDP-ManNAcA, 50 mM HEPES pH 8.2, 20 mM magnesium acetate, 2 mM 2-mercaptoethanol, 9 to 35 mg of cell wall acceptor per ml, and 0.15 to 15 g protein per ml. The cell wall acceptor refers to the purified TUA preparation (a short, soluble form of TUA) which was originally released from the M. luteus cell wall by treatment with acid. This soluble acceptor was found to be capable of accepting glucose and ManNAcA and facilitating the elongation of the TUA chain [6].
The reaction was stopped by adding 20–30% (v/v) concentrated isobutyric acid. The radioactive product was separated by paper chromatography in isobutyric acid: 1 M NH4OH (5 : 3 v/v). The product at the origin of the paper was quantitated by liquid scintillation counting. It had previously been analyzed by mass spectrometry, nuclear magnetic resonance imaging (NMR), and carbohydrate PAGE and had been confirmed to be teichuronic acid [2, 9]. In addition, the enzymatic products were also analyzed with a preparative nonreducing polyacrylamide gel electrophoresis followed either by alcian blue/silver staining or autoradiography [6, 8, 10].
2.4. Physical and Chemical Properties of TUAS
The effect of different incubating conditions and reagents on the TUAS enzyme activity were studied (such as enzyme substrates, growth phases, detergents, and phospholipase treatment). Other physical and chemical properties of purified TUAS were also studied including density, hydrophobicity, mobility, optical properties, isoelectric point, physical form, and subcellular distribution.
2.5. Lipids and Pigment Analysis
The optical properties (including pigments) of the purified active fraction(s) were analyzed by spectrophotometry, with wavelengths ranging from 200 nm to 700 nm. The same fractions were also subjected to phase partition with solvent mix (Chloroform : Methanol : distilled water; 8 : 4 : 3, v/v/v). The lower organic phase was extracted and per-methylated. The chemically derivatized product was analyzed on a GC-MS (HP 6890 gas chromatograph/HP5973 MSD) with a DB-17 capillary column at a constant flow rate of 1 ml/min [11].
2.6. Immunologic Assays
Antiserum to TUAS was raised in New Zealand White rabbits. Immunoblot analysis (Western blot) was performed. Immunofluorescence labeling was performed by incubating cells of M. luteus with primary antibody (serum) followed by goat antirabbit IgG-FITC conjugate. Labeled cells were observed with a differential phase contrast fluorescent microscope.
3.1. TUAS Is a Bifunctional Glycosyltransferase
The purified enzyme fraction displayed the typical reaction for glucosyltransferase, which is the transfer of [14C]glucose from UDP-[14C]glucose to the teichuronic acid acceptor. However, the enzyme is also capable of incorporating ManNAcA into the same polysaccharide. Adding 0.5 mM UDP-ManNAcA in addition to 0.5 mM UDP-glucose can significantly increase the rate of teichuronic acid biosynthesis by 400% (Figure 2(a)). The enzymatic products were analyzed by Native-PAGE, which revealed a typical ladder pattern for linear polysaccharide with one repeating unit or two sugars apart (Figure 2(b)).
(a) Effect of the two substrates (UDP-[14C]glucose and UDP-ManNAcA) on the activity of teichuronic acid synthetase (TUAS). Open circle: with one substrate 0.5 mM UDP-C14-Glucose; Closed circle: two substrates by adding 0.5 mM UDP-ManNAcA to the same mix. (b) Analysis of teichuronic acid, the enzymatic product of TUAS, by nondenaturing PAGE stained with Alcian blue and silver. The numbers on the right represent the repeats of the basic TUA disaccharide unit. D is an oligosaccharide of TUA estimated to have 6–10 disaccharide repeats, which is not detectable by PAGE.
The GC-MS analysis of the same enzymatic product hydrolyzed with trifluoroacetic acid (TFA) showed two component sugars: Glucose and ManNAcA. These results indicated that efficient biosynthesis and elongation of teichuronic acid polymer by purified TUAS requires both UDP-ManNAcA and UDP-Glucose. Or in other words, TUAS is a bifunctional glycosyltransferase capable of transferring both the component sugars (Glucose and ManNAcA) for the TUA polymer.
3.2. TUAS Is a Multi-Subunit Enzyme Complex
The TUAS activity is always associated with a large protein of molecular mass 440 KDa (Figure 3(a)). This protein can be further separated by SDS PAGE into two small protein subunits A and B with molecular mass equivalent to 54 kDa and 52.5 KDa (Figure 3(b)). No TUAS activity was detected from these two small proteins even after SDS removal. Enzymatic activity was detected from a protein band on a native gradient PAGE. The band did not look very sharp. When exposed to prolonged electrophoresis, the TUAS band became fainter and fainter, while a wavy band appeared and migrated to the bottom of the gel. The wavy band did not have enzymatic activity but contained the 54 kDa and 52.5 kDa subunits. This result indicated that TUAS is an enzyme complex composed of an octomer (two tetramers), which assembled in a highly ordered fashion. When the 8 subunits disassociated, the protein lost its conformation as well as the catalytic function for TUA biosynthesis.
(a) M. luteus TUAS analyzed with native gradient PAGE. Partially purified TUAS was subjected to electrophoresis on 3–12% native gradient polyacrylamide gels (left, lane 2). Protein bands were visualized by staining with Coomassie blue. The molecular-mass standards of 545, 272, 132, and 66 kDa (top to bottom) are shown (left, lane 1). The TUAS activity is indicated with an arrow. (b) SDS-PAGE of M. luteus TUAS. Protein bands separated by 9.5% SDS-PAGE were visualized by silver staining. Lane 1: Molecular-mass standards of 97.4, 66.2, 42.7, and 31 kDa, respectively (top to bottom). Lane 2: Detergent extraction of membrane fraction. Lane 3: Protein after DEAE-cellulose column chromatography. Lane 4: TUAS purified to near homogeneity by isoelectric precipitation (pH 5.0) after DEAE-cellulose, gel filtration and adsorbent column chromatography. TUAS has two subunits A and B, upper subunit (A) is equivalent to 54 kDa and the lower subunit (B) to 52.5 kDa.
3.3. TUAS Possesses Hydrophobic Properties and Its Function Is Associated with the Cytoplasmic Membrane
(a) Low Density
Fractionation of Thesit-solubilized membrane fraction with ammonium sulfate (25%, w/v) results in the formation of a protein precipitate which can be collected by sedimentation. But very little TUAS activity (5%) was detected from the pellet or from the soluble supernatant (16%). The majority (70%) of the enzymatic activity was found in a low density layer which rises to the top of the tube during centrifugation. This layer contained detergent and lipids derived from the membrane as well as TUAS. The specific activity of TUAS in the lipid/detergent layer was increased by more than 3-fold over the original detergent-solubilized membranes (Table 1).
TUAS
Fraction Activity protein Specific activity
(units) (%) (mg) (%) (units/mg protein)
Original extract 126 100 18.0 100 7.0
Top lipid layer 89 71 3.8 21 23.0
Supernatant fraction 20 16 9.6 53 2.1
Precipitate (pellet) 6 5 4.7 26 1.3
TUAS activity found in fractions after partitioning with 25% ammonium sulfate.
(b) Pigments and Lipids
The active fractions of TUAS are usually associated with a yellow color. Carotenoids are the characteristic pigments of the cytoplasmic membrane of M. luteus [12]. Even after extensive purification, the TUAS contains a pigment which is visually observed as a yellow-green color with absorption maxima at 300, 385, and 415 nm. The pigments and membrane lipids [13] are readily extracted from the enzyme by organic solvents such as chloroform and 1-butanol. However the enzyme lost activity after solvent extraction.
(c) Formation of Vesicles or Micelles
The TUAS possesses unusual hydrophobic properties which suggest that it readily forms vesicles. Fractionation of detergent-solubilized samples by gel filtration has been uniformly disappointing. Usually the amount of enzyme activity recovered is severely reduced. When activity is recovered, the elution position has always been at the excluded volume of the column, suggesting that the TUAS is not behaving as a soluble protein but rather exists in micelles or vesicles. Pigmented vesicles or micelles were observed through all purification and characterization procedures for this TUAS study.
(d) Effect of Phospholipase C
To understand whether the membrane lipids associated with the enzyme are essential for TUAS activity, the purified TUAS was treated with exogenous phospholipase C. The time course in Figure 4 showed a rapid (15 minutes) and significant ( 90%) inhibition of TUAS activity by phospholipase C. After 60 minutes of phospholipase treatment, artificial phospholipid vesicles (Sigma) were added to the TUAS reaction mix. Interestingly, a partial recovery of TUAS activity was observed (Figure 4). These results suggest that the membrane lipids associated or surrounding the TUAS enzyme complex play an important role in enzyme catalytic function.
Time course of TUAS activity of M. luteus and the effect of phospholipase C on the activity. Open circle: TUAS activity; Closed circle: TUAS treated with phospholipase C; Triangle: addition of artificial phospholipid vesicles to TUAS reaction mix following phospholipase treatment.
(e) TUAS Activity at Different Subcellular Compartments and Detergent Enhancement
Four subcellular compartments of M. luteus were prepared by physical grinding (without using lysozyme). These included cytoplasm, cytoplasmic membrane, cell wall, and culture supernatant (cell filtrate). The fractions were standardized based on the protein concentration. The enzymatic activity of TUAS was analyzed in those fractions and control medium (before culturing bacteria). Table 2 is the distribution of specific activity, in which cytoplasmic membrane contained the highest total and specific TUAS activity. The enzyme activity was also found in the cell wall fraction (6 units/mg of protein). Very little activity could be detected in cytoplasmic fractions. The culture supernatant contained yellow colored membrane vesicles and displayed a higher specific activity (8.7 units/mg of protein) of TUAS indicating that even in intercellular space, TUAS is embedded in the vesicle membrane and capable of catalyzing the polymerization of TUA polymer. However, it is unclear whether this is a life cycle dependent process. The TUAS is readily solubilized from membrane fragments by washing with 3 to 20% detergent, such as Thesit or CHAPS. Application of detergent also increases the specific activity in some of the cellular fractions. Antiserum to TUAS was raised in rabbits. Immunoblotting showed that the enzyme was mainly associated with the membrane fraction. Figure 5 showed that intact M. luteus cells bound substantial amounts of the antibody as detected with an immunofluorescent assay, indicating that some TUAS is readily detectable from outside the cell wall as an extracellular protein.
Cellular compartment Specific activity (units*/mg protein)
Control medium 0
Culture supernatant 8.7
Cytoplasm (S-20 fraction) 0.5
Cell wall ** 6.2
Cytoplasmic membrane** 19.9
* 1 Unit 1 nmole [14C]glucose incorporated in 60 minutes in standard assay.
** Separated by sucrose density gradient centrifugation.
Distribution of TUAS activity in subcellular extract of M. luteus.
Immunoflluorescent images of M. Luteus. For (a) and (b), cells were observed under a fluorescent microscope with excitation wavelength 495 nm and emission wavelength 520 nm. (a) a negative control in which M. luteus cells were incubated with the secondary antibody conjugated to FITC. (b) M. luteus cells were incubated with both anti-TUAS serum and the secondary antibody conjugated to FITC. (c) The same bacterial cells as (b) except under visible light.
Proposed mode of action and subcellular location for cell wall TUA biosynthesis, in which an enzyme complex, TUAS, consisting of two kinds of enzymes (Glucosyltransferase and ManNAcA-transferase), serves as a multitasking polysaccharide assembling station on the bacterial membrane for efficient elongation of cell wall teichuronic acid. Black Diamond: ManNAcA, White Circle: glucose, Rectangle: linkage oligosaccharide, and Yellow Circle: phosphate.
Bacterial surface polysaccharides are essential for bacterial survival. They play important roles including protection of the bacterial cell, signal transduction, nutrition regulation, and interaction with the environment as well as the host defense system. Consequently, there is increased interest in understanding the unique polysaccharide structures responsible for such interactions, as well as their biosynthetic origin, and ultimately, the mechanisms which control and regulate their synthesis. Recently much effort has been directed toward identification of the genes and gene products responsible for cell surface polysaccharide biosynthesis [14–16].
M. luteus is not a severe pathogenic bacterium, however for many years it has served as the model system for bacterial cell wall study. The TUA polymer of M. luteus is acidic and has some similarity with that of the so-called capsular polysaccharides (CPS) which are usually considered to be essential and virulent factors for pathogenic bacteria, such as Streptococca and Staphylococca [16–19].
Biosynthesis of polysaccharide requires glycosyltransferases, each of which transfers a specific sugar from an activated donor molecule, usually a nucleoside-diphospho-sugar, such as UDP-glucose, to an acceptor. Synthesis occurs either by sequential addition of residues to a growing polysaccharide chain or by assembly on a carrier lipid [20, 21] of an oligosaccharide unit which subsequently is polymerized. These enzymes are likely located in the cytoplasmic membrane. Although the activities of many such enzymes have been known for decades, and many genes of glycosyltransferases have been identified and expressed, purification of such functional membrane-associated enzymes in cell-free systems has progressed slowly. While many bacterial glycosyltransferase genes were identified through phenotype assays or homology searches, their gene products were, unfortunately, very hard to express as active enzymes. This may be due to a lack of the secondary modifications of the gene products, and the complexity of polysaccharide biosynthesis. In this study, through a delicate enzymologic approach, a membrane associated enzyme, teichuronic acid synthetase (TUAS), was purified from a gram-positive bacteria, Micrococcus luteus. Based on the experimental data obtained through this study, a mode of action model is proposed in Figure 6, which gives a unique interpretation of the topology of bacterial surface polysaccharide biosynthesis.
The features of this model are as follows. (1) The four subunits of the Glucosyltransferase and the four subunits of the ManNAcA-transferase are assembled (in an alternating order) into an octomer, which forms a circular enzyme complex arranged like the segments of an orange. (2) The octomeric enzyme complex resides in the cytoplasmic membrane of gram-positive bacteria, with the catalytic domain in the center. (3) The enzyme can accept the sugar donors of either NDP-sugars or glycosyl carrier lipids [20, 21] from the cytoplasmic side and link the sugar to the nonreducing terminus of the existing TUA polymer, which is presumably covalently anchored to the cell wall peptidoglycan through an oligosaccharide and a phosphodiester bond. The reducing terminus of the linkage region, or that of the entire TUA chain, is a GlcNAc residue [3, 4]. (4) Each subunit of the enzyme is likely capable of adding one corresponding sugar, so after one round of catalysis, 8 sugars or an octosaccharide will be added to the existing polysaccharide chain and be squeezed out of the cytoplasmic membrane to the cell wall region or extracellular space. (5) In this model, no transporter, membrane porins and pumps are required. The TUAS is able to transfer two different sugars in alternating order, polymerize the disaccharide repeating units, transport the synthesized chain to the cell wall and protect the membrane integrity. The TUAS enzyme complex together with the surrounding membrane lipids serves as an efficient multitasking polysaccharide assembling station on the bacterial membrane for efficient elongation of cell wall teichuronic acid (Figure 6).
Further study is needed to understand the assembling of the enzyme complex, the TUA polymer's attachment to the cell wall, and the other important component factors within the complex, as well as the expression and regulation of the gene operon encoded for TUAS. This knowledge will be very useful and important in understanding the mechanism of extracellular polysaccharide biosynthesis, as well as developing antibiotics against similar enzymes in pathogenic gram-positive bacteria other than M. luteus.
The authors thank Dr. Jocelyn Shaw, University of Minnesota, Department of Genetics, Cell Biology and Development, for technical advice and guidance regarding immunofluorescent microscopy. The authors thank Ken Campbell and Leo Xiaoyang Liu for technical assistance. This research was supported by Public Health Service Grants AI-08295 from the National Institute of Allergy and Infectious Diseases, and by a research Grant RG-107-N from the American Lung Association.
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OREANDA-NEWS. August 23, 2013. Plains All American Pipeline, L.P. (NYSE: PAA) and PAA Natural Gas Storage (NYSE: PNG) announced that they have closed the renewal and extension of their principal bank credit facilities. PAA also announced today that the company has established an unsecured commercial paper program on a private placement basis.
PAA renewed two credit facilities: a USD1.6 billion, five-year senior unsecured revolving credit facility and a USD 1.4 billion, three-year senior secured hedged inventory facility. The maturities associated with these facilities represent two-year extensions of previous facilities, which now mature in August 2018 and August 2016, respectively. Both facilities contain accordion features that permit PAA (subject to receipt of incremental lender commitments) to increase borrowing capacity to USD 2.1 billion and USD 1.9 billion, respectively.
PNG extended the maturity of its USD 550 million, five-year senior unsecured credit facility by one year. The facility now matures in August 2017. The credit facility includes a USD 200 million Gulf Coast Opportunity Zone (GO Zone) tax-exempt term loan and a USD 350 million revolving credit facility. The revolver includes an accordion feature that permits PNG (subject to receipt of incremental lender commitments) to increase borrowing capacity to USD 550 million.
Bank of America, N.A. will serve as Administrative Agent for the facilities. Merrill Lynch, Pierce, Fenner & Smith Incorporated served as Joint Lead Arranger for the facilities and was joined by Citigroup; DNB; J.P. Morgan; Societe Generale; SunTrust Robinson Humphrey; and Wells Fargo Securities, LLC as Joint Lead Arrangers on one or more of the facilities. The new credit facilities became effective on August 16, 2013.
Pursuant to the commercial paper program, PAA or its indirect subsidiary Plains Midstream Canada ULC ("PMC") may issue, from time to time, unsecured commercial paper notes up to a maximum aggregate amount outstanding at any time of USD 1.5 billion. The notes will be backstopped by PAA's revolving credit facilities, and any commercial paper notes issued by PMC will be guaranteed by PAA. The proceeds from the issuance of the notes will be used for general partnership purposes.
"We appreciate the continued strong support from our bank group," said Al Swanson, Executive Vice President and CFO of Plains All American and PAA Natural Gas Storage. "In addition to our USD 1.6 billion 2013 capital program, PAA has a large portfolio of organic growth projects and remains active in pursuit of acquisition opportunities. These facilities, along with the commercial paper program, support Plains' strong liquidity, enabling substantial financial flexibility to execute our growth plans."
The notes to be offered under the commercial paper program will not be registered under the Securities Act of 1933 and may not be offered or sold in the United States absent registration or an applicable exemption from registration requirements. This press release shall not constitute an offer to sell or the solicitation of an offer to buy notes under PAA's commercial paper program.
Plains All American Pipeline, L.P. is a publicly traded master limited partnership engaged in the transportation, storage, terminalling and marketing of crude oil and refined products, as well as in the processing, transportation, fractionation, storage and marketing of natural gas liquids. Through its general partner interest and majority equity ownership position in PAA Natural Gas Storage, L.P. (NYSE: PNG), PAA owns and operates natural gas storage facilities. PAA is headquartered in Houston, Texas.
PAA Natural Gas Storage is a publicly traded master limited partnership engaged in the development, acquisition, operation and commercial management of natural gas storage facilities. The Partnership currently owns and operates three natural gas storage facilities located in Louisiana, Mississippi and Michigan. The Partnership's general partner, as well as the majority of the Partnership's limited partner interests, is owned by Plains All American Pipeline, L.P. (NYSE: PAA). PNG is headquartered in Houston, Texas.
Устюгов поделился своим мнением о КлебоSport.ru | 12.12.2021 01:33:37

redpajama_set_name: RedPajamaCommonCrawl


text:
Security Researcher Breaks Google's Bug Database, Lands $15,600 Bug Bounty
Alex Birsan, a security researcher, gained entry into Google's internal bug tracker -- reaching some of the company's most compromising vulnerabilities.
by D. Howard Kass • Nov 1, 2017
Pocket a hefty bounty for breaking something…we should all be so industrious. Alex Birsan, a security researcher, appears to have been smart, resourceful and persistent enough to trick Google's internal bug tracker into gaining entry to thousands of some of the company's most compromising vulnerabilities.
For his 17 hours of unsolicited work (more on that below), Google shuttled a cool $15,600 in bounty Birsan's way along with the appropriate gratitude for alerting it to the three process vulnerabilities he discovered. "Easy bugs for hard cash," Birsan called it on a blog post (via ZDNet). "I'm very happy with the extra cash, and looking forward to finding bugs in other Google products."
For the uninitiated user, which in this case is most of us save developers or Google staffers, the company uses an Issue Tracker, aka Buganizer System tool, to track bugs and feature requests that turn up in product development. Birsan noticed that his vulnerability reports were being handled by opening a new thread in the Google Issue Tracker as well as by sending him an email.
"Naturally, I immediately started to break it," he said. "We, as external users, only get to see the tip of the iceberg: A small set of pre-approved categories, and issues where someone at Google explicitly added an external account, such as vulnerability reports. But how much information lies under the surface?"
By his calculations, Birsan had hit upon a Google treasure trove of vulnerabilities information that, if compromised by a hacker, could create havoc for the company. Some 2,000 to 3,000 issues are opened during working hours, with only 0.1 percent public, he estimated. "Seems like a data leak in this system would have a pretty big impact."
Here, his own words, is the step-by-step of Birsan's caper (an interesting full read on his blog, here abridged):
Bug #1: One of the first things I noticed upon discovering the issue tracker was the ability to participate in discussions by sending emails to a special address.
The next best thing I could think of was getting a Google account with an @google.com main email address, which would hopefully give me some extra privileges on the Buganizer. Registering such an account from outside Google was not supposed to be allowed. However…if I signed up with any other fake email address, but failed to confirm the account by clicking on a link received by email, I was allowed to change my email address without any limitations.
Soon after, I received the confirmation email as a message on the corresponding issue page:
I clicked the confirmation link, logged in on the Issue Tracker, and I got redirected to the corporate login page. And no, my Google account credentials did not work there. Nevertheless, this account gave me a lot of extra benefits in other places across the internet, including the ability to hitch a ride (for free, maybe?), so it was still a security problem that opened a lot of doors for malicious users.
Bug #2: The ability to star items…means you're interested in the problem being discussed and you want to receive email notifications whenever someone adds a comment. The interesting thing I noticed about this functionality was the distinct lack of errors when trying to use it on issues I did not have access to.
I logged in to my second account and tried to star a vulnerability report from my main account by replacing the Issue ID in the request. (He was successful). Could it be that easy to spy on open Google vulnerabilities? I quickly posted a comment on the issue to see if I my fictional attacker account would get notified about it.
But again, no email ever showed up. So I got a recent Issue ID, and extrapolated a range of a few thousand IDs which should coincide with the latest issues in the database. I then starred them all. (His inbox was flooded in minutes).
My first thought when opening the inbox was "Jackpot!" However, upon closer inspection, there was nothing particularly interesting going on in those threads.
Bug #3: When you visit the Issue Tracker as an external user, most of its functionality is stripped away, leaving you with extremely limited privileges. If you want to see all the cool stuff Google employees can do, you can look for API endpoints in the javascript files. When designing this limited version of the system, someone was nice enough to leave in a method for us remove ourselves from the CCs list if we lose interest in an issue or simply don't want to receive emails about it any more.
However, I noticed some oversights here…There was no explicit check that the current user actually had access to the issues specified…If you provided an email address that was not currently in the CCs list, the endpoint would return a message stating the email had been removed successfully…If no errors occurred during the action, another part of the system assumed that the user had proper permissions.
Obviously, I could now see details about every issue in the database by simply replacing Issue Ids in the request…Bingo!
"When I first started hunting for this information leak, I assumed it would be the Holy Grail of Google bugs, because it discloses information about every other bug," Birsan wrote. "However, after finding it, I quickly realized that the impact would be minimized, because all the dangerous vulnerabilities get neutralized within the hour anyway."
No matter, his pockets are a bit heavier now for the effort.


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Media Inquiries & Logo Library
Arkansas Data Center
Community Development & Planning
Economic Research & Data Analysis
Geographic Information Services
Category: January 2021
Environmental study recommends new, direct route to XNA
An environmental assessment found that a proposed access road to the Northwest Arkansas National Airport shouldn't significantly affect threatened or endangered species or environmentally sensitive
State jobless rate hit 4.2% last month; Arkansas' figure 9th-lowest in U.S.
Arkansas' unemployment rate dropped to 4.2% in December, the second-best improvement in the nation. Arkansas now has the ninth-lowest unemployment rate in the nation. Because
Steep increase reported in Arkansas job numbers; December jobless rate falls to 4.2%
Arkansas added more than 65,000 jobs between November and December. The state's jobless rate dropped from 6.3% to 4.2% in December. However, Michael Pakko is
How President Biden's new relief plan could help Arkansas's economy
Dr. Michael Pakko was interviewed about how President Biden's 2 trillion dollar relief plan and new stimulus checks could help Arkansas's economy.
What impact could a $15 minimum wage have on Arkansas workers?
The Biden Administration is looking at proposing a $15 federal minimum wage increase. Arkansas' minimum wage is currently $11 an hour, much higher than the
Pandemic pauses recent gains in Arkansas' manufacturing sector employment
Manufacturing in Arkansas struggled to grow for more than a decade, then finally saw improvement in 2018, which continued until the pandemic hit. Dr. Michael
Factory sector starts off year strong in state
Arkansas' manufacturing sector had a strong start in 2021, with four major manufacturing operations choosing to stay in Arkansas instead of moving elsewhere. The decision
Pandemic revenue crunch short-lived in the city, county
Though the pandemic has brought economic struggles to most communities, Hot Springs and Garland County are seeing increases in their revenue. "The strength of sales
Latest Arkansas Revenue Report Shows Continued Above Forecast Growth
Arkansas' economy continues to outperform its forecasts, according to the December revenue report from the Department of Finance and Administration. Arkansas' net available general revenue
grow@youraedi.com
©2020 Arkansas Economic Development Institute. All rights reserved.
A special thanks to Formation PR + Brand for the development of this website on behalf of AEDI and the people of Arkansas.


It's time to conquer Gamindustri, one city at a time. With the Mega Nepgeardam's poseable limbs, this robot's flexible enough to defeat any other plushie in a battle.
Click the button below to add the Mega Nepgeardam to your wish list.


text:
Crawler Group Releases New Version of Its Popular Free Internet Security Application - Web Security Guard 1.5
New 1.5 version enhances free Web Security Guard Internet threat prevention capabilities by alerting users of potentially harmful websites with more languages, website ratings and new user account management.
Boca Raton, FL - August 6, 2007 - Crawler Group, provider of free Crawler software, announces the release of new Web Security Guard 1.5, a free powerful Internet threat prevention application. Riding the wave of success since Web Security Guard's initial release, the company has quickly produced new enhancements to further evolve the product and increase user security and safe browsing on the Internet.
Additionally, Web Security Guard 1.5 becomes a heavy weight contender in the industry when coupled with its sister product Spyware Terminator 2.0 antispyware, producing a totally free, full Internet security suite available to consumers and businesses. The key enhancements of version 1.5 include:
Multiple Language Support - Web Security Guard installer, application and website reports have been translated from English into Portuguese, Spanish, Czech, Brazilian Portuguese, Italian, French and German with other languages following soon
New User Account Management - Web Security Guard enables users to create their user account and publish their reviews under their name or nickname
Database of Rated Websites Extended - the number of website ratings in Web Security Guard's database has doubled since the previous release
Web Security Guard Database Integration with Spyware Terminator 2.0 - Web Security Guard's database of website ratings powers new features of Spyware Terminator including Internet protection, cookies and favorites scans, providing full Internet security to users
Improved Updates Interface - users can check the progress of the update process in real-time
New Settings Dialog Interface - settings window for Microsoft® Internet Explorer® and Mozilla® Firefox® has been unified into one user preferred mode
Performance Improvements - additional improvements have been applied to boost Web Security Guard's overall performance
The new user account management tool was built as the precursor of a new long-term website rating program whose infrastructure is currently under construction. The user account creation is the first step towards an easy-to-use comprehensive website rating facility which Web Security Guard's user community urged to have implemented.
"Web Security Guard 1.5 is a very important release for the product's future. Version 1.5 lays the foundation on which a multilingual Web Security Guard community can grow," said Robert Österlund, CEO. "Our efforts in building and supporting a good quality user base and its website rating activity will directly influence the quality of Web Security Guard's protection level."
Portuguese, Spanish and other languages will make Web Security Guard accessible to many non-English speaking users. Supporting Microsoft® Internet Explorer® and Mozilla® Firefox®, Web Security Guard is freely available at its www.websecurityguard.com website. Additionally, Web Security Guard is also offered bundled with Spyware Terminator, creating a totally free, full Internet security software suite for consumer and business use and is available on the Spyware Terminator website at .
About Crawler Group
Crawler Group is a leading innovator of search technology and software applications focusing on rich, interactive experiences and safety for consumers and businesses. Crawler products are meticulously developed and are highly ranked by industry experts and users alike. The company is dedicated to the idea that everyone worldwide should have access to free software. Crawler Group is one of a family of companies in the Xacti Group. Xacti has a global mission to create and operate a diversified portfolio of scalable businesses through the innovative use of technology. To learn more, visit www.crawler.com and www.xacti.com.
Ellen Rowley,
Note to editors: Crawler, Spyware Terminator and Web Security Guard are trademarks of Crawler Group. Mozilla and Firefox are registered trademarks of the Mozilla Foundation. Microsoft and Internet Explorer are registered trademarks of Microsoft Corporation. Other company or products mentioned herein are trademarks or registered trademarks of their respective companies.
software applications focusing on rich, interactive experiences and safety for consumers and businesses. Crawler products are meticulously developed and are highly ranked by industry experts and users alike. The company is dedicated to the idea that everyone worldwide should have access to free software. Crawler Group is one of a family of companies in the Xacti Group. Xacti has a global mission to create and operate a diversified portfolio of scalable businesses through the innovative use of technology. To learn more, visit www.crawler.com and www.xacti.com.


This estate is sold with a new hand-cut stone house amidst the olive grove and intact nature and two ruins that allow the construction of two more residential buildings, all in an attractive location on the hills of the island.
On the plot there is a new built stone house with a total surface of 170 m2, with ground floor and first floor.
It has four bedrooms, living room with kitchen, bathroom, auxiliary toilet, storage and a covered terrace.
The house is very well equipped and decorated. All furniture is made of teak and carefully selected.
This property offers a total of 4000 sqm of land around the house and has a permit to build two more properties, one of 108 sqm and the other one of 188 sqm, due to the two ruins that are currently on the plot.
A little further away from the house there is another big well-groomed olive grove that has over 6000 m2 and gives plenty of fruit and top quality oil.
The terrain is straight, right shape and maintained. Electricity, water /water tank), septic tanks are solved in a proper way.
Two plots are not connected but are close by (walking distance).
It's an excellent property for a real vacation surrounded by untouched nature and greenery, ideal for relaxing and enjoying one of the most beautiful islands in Dalmatia close to the city of Dubrovnik.
The price of this realestate is 550 000 euros.


Do you have foods that you can eat in one form but not another? For example, cooked oatmeal is really easy and soothing for my stomach, but baked oatmeal (like granola) gives me terrible stomach cramps. I can eat scrambled eggs, but if I eat boiled or fried eggs, where the yolk is separate, I feel sick. I can eat plain bread, but a muffin will make me sick for days (I can't figure out what ingredient would be in it that would make me so sick).
Yes, absolutely. I can eat cheese but not yogurt. I haven't had raw veggies for years - and I used to be quite the salad eater - but I can have cooked, though never broccoli and not much in the way of Brussels Sprouts or cauliflower, either.
I finally figured out that if I stick to mostly soluble fiber, I'm ok. Insoluble fiber just makes me constipated. Gluten free eating also made me constipated!?
Fibromyalgia, degenerative disc disease, discectomy L4-L5 - (w/lots of Sciatic Nerve damage), frozen shoulder, Hashimoto's Thyroiditis, IBS, migraine, dizziness (mostly from visual stimuli), elevated liver enzymes, tachycardia, hearing loss (probably Menieres).
It may not be the oatmeal but another ingredient in the granola. Keep a Food Journal - see a zillion posts in the archives, aka the search box at the top right of the page, aka "google custom search."
Several years ago my allergist had me keep a journal and I found my "trigger foods," which led me to not the whole hamburger but the condiments which conatined vinegar, and led me to sulfites. Not that this is your trigger, but it's a way of finding your own.
I've experienced the same sort of sensitivities over the years and what has helped me the most is when I watched an author/nutritionist JJ Virgin speak on PBS. She has a book out about eliminating 7 types of foods from your diet for 3 weeks to see which ones you're sensitive to then reintroducing them one at a time. It worked for me. Sure enough some of the foods that I reintroduced caused a big reaction like increased pain or digestive issues and issues with trying to get adequate sleep.
I can't do caffeine. So I stay away from caffeinated products especially chocolate.
I still have a tough time with peanuts, sugar, dairy, and gluten so I rarely eat them. I eat Ezekial bread. It's a sprouted bread located in the grocery store's freezer section and suppose to be more healthy than whole wheat. It also has a lot of fiber. You mentioned how a muffin affects you. Maybe it doesn't have much fiber or the sugar might be affecting you? The baked oatmeal wouldn't work for me. I do have to make sure that my daily morning breakfast of steel cut oatmeal made with various seeds and nuts and topped with frozen bluesberries after it's microwaved each morning isn't too thick. I make enough for 5 days at a time.
Ha! I know that feeling exactly!
Yes I have weird food issues! My problem is mostly with meats- they often taste spoiled- but there is no rhyme or reason to what I can or can't eat. I don't usually have as much trouble with fruits and veggies or most seafood. Once in a while I may be able to eat a little meat or something I usually have trouble with- even if it was always a favoirite in the past and the next day or next MEAL I can't eat it. Feel like I'll throw up if I swallow it. I usually stick to the same few foods I know I don't have trouble with. Can't eat meat on pizza- if i can eat the pizza at all. Spicy foods go better. There is only one restaurant where I can eat a burger and then only half of it. Can't even eat burgers I make myself. It's very frustrating! I find something that goes well and the next time I can't eat it. On the bright side- I'm losing weight. 😀 Seriously though I have to make an effort to get a balanced diet and enough fluids- feel nauseated if I drink too much of anything at one time. I eat bars high in protein so i get enough protein. So thankful I have a supportive and understanding husband and family!
It's possible it's more of a gut issue than fibro although I know fibro can cause it too. Many foods can mess the body up if you do.
What if trials of this life are Your mercies in disguise.
FM/CFS, BP, gastritis, diverticulitis, anxiety/PTSD, adult ADD, hypothyroid, brain lesions, sleep apnea that doesn't respond to a c-pap as far as sleepiness/fatigue goes, insomnia and only sleep in stages 1 and 2 and REM with a tiny bit in 3 and 4.
My husband is allergic to almost everything. (Think Bubble wrap needed) He can have eggs, pan fried without lots of oil, scrambled, omelet, quiche, and in baked goods, but boiled eggs make him sick as can be.
He has to be off of sulfites and sulfa, and sulfates............something in the chemistry of the egg changes and makes him very ill when boiled.
I can't eat the vegetable corn .........yet I can eat a few 100% corn chips and I don't seem to react to corn starch..........corn makes me feel like dying would be better. I just can't digest it and it is so painful until it passes......even creamed corn.
We have to be gluten free and oats made us both double over in gastric pain......... I discovered that unless it is declared GLUTEN FREE Oats use the same grinding stone for wheat.
My husband is highly allergic to corn....... he was reacting to everything. salt, tea, paper plates and cups, coffee. I researched for ever to find out that the table salt I was using uses corn to process the iodine into it and to keep it pouring freely. The tea bags, the coffee filters and paper plates and cups have corn in the process of making them.
Sometimes it is searching for a needle in a haystack to find the triggers.


Texas Taxpayer Number assigned to DON JUAN FOOD SERVICES, LLC is 32038646090. Texas SOS File Number of this company is 0801072418. This company state of formation is Texas.
DON JUAN FOOD SERVICES, LLC mailing address is 15100 ELLA BLVD APT 1306 HOUSTON, TX 77090-7036. Registered office street address is 15100 ELLA BLVD., APT. 1306 HOUSTON, TX 77090. You can find this business by geo coordinates: 29° 59' 10.6" N , 95° 25' 51.5" W.
DON JUAN FOOD SERVICES, LLC was incorporated on Friday 9th January 2009, so this company age is ten years, three months and fourteen days. Company right to transact business in texas is currently FRANCHISE TAX INVOLUNTARILY ENDED.
DON JUAN FOOD SERVICES, LLC agent is FRANCISCO A. MATTEI. Company has one officers: FRANCISCO A. MATTEI employed as managing m. Check more don companies.


text:
You Are Safe, Little Ones, by Janice Canerdy
Guardian Angel and Children Crossing Bridge, by H. Zabateri* (Austria), 1918.
You Are Safe, Little Ones
I see a footbridge high above a gorge.
One bannister is gone; the other lies
on narrow rotting boards. Rough waters surge
beneath this passageway that creaks and sighs
in answer to footfalls of children who,
while clinging to each other, move ahead
with wary steps toward home and suppertime
and hope they'll soon be safely tucked in bed.
These innocents are not alone. Unknown
to them, an angel stands close by to keep
them safe from peril that could plunge them to
the depths. Tonight no one will grieve and weep.
Janice Canerdy
Janice Canerdy is a retired high-school English teacher from Potts Camp, Mississippi. Her poems have appeared in various magazines, journals, and anthologies. Her first book, Expressions of Faith (Christian Faith Publishing, 2016), may be purchased online through Amazon and Barnes and Noble.
*Editor's note: This famous painting of children crossing a bridge, protected by a guardian angel, is familiar to countless people whose childhood bedrooms included a print of the work, like a night light, or whose picture Bibles and Sunday Schools featured the art. There is much confusion over the artist, often listed as Lindberg Heilige Schutzengel, or sometimes as "Heilige Schutzengel by Lindberg." Heilige Schutzengel means Holy Guardian Angel in German, and is a reference to the content of the painting, but Linberg was one of the poster printers for this work, not the artist's name. H. Zabateri was an Austrian academic painter of mythological and religious scenes; however, he also did not exist and was a pseudonym for Hans Zatzka. In turn, Zatzka also used Pierre de Ronsard, Joseph Bernard, and Bernard Zatzka, adding to the tangle. The purpose behind the artist's multiple identities was probably, in part, eccentricity, but also pragmatic: he was extremely prolific, and contracts limited how many works he could legally sell, so one way to circumvent that was to paint under different names.
Isabel Maria Cabello Sibaja
Tengo información de un cuadro igual que éste firmado con el nombre de "Zabateri".
Dónde puedo obtener información de su autenticidad, valor?


text:
The Path Forward: A Terminal Manager's Playbook to Create a Soaring 2020s
by Jory Weissman | Jan 8, 2021 | Airport | 0 comments
We're ten precent of the way into the 2020s, and for those in the travel and tourism industry, there's only one way the rest of the decade can go. It's important to remember that travel will come back. Maybe not today, maybe not early in 2021, but terminals will once again be packed, airplanes will be full, and the airport will once again see the hustle and bustle it did in 2019.
Recovery is Coming… But When?
It took about six years for airlines to recover capacity after the 9/11 terrorist attacks, a time in which the fallout resulted in 62,000 airline jobs lost. But unlike the 2020s, the 2000s were a series of unfortunate events. Before 9/11, the dot-com bubble burst left business travel waning. After it, travel had to mitigate the damage of the SARS outbreak, the Avian Flu outbreak, and the global financial crisis.
Though COVID-19 resulted in faster, deeper, and more significant cuts—some believe that the return to some semblance of normal might come sooner rather than later. Despite IATA data highlighting that it generally takes at least five years for the industry to recover after a short-term upheaval, four in ten believe that recovery could come in as little as 18 months.
Whether it's cautious predictions of the mid-20s or something a bit more optimistic, those in charge of terminals need to be ready for whatever the coming decade throws at them.
While we can expect the new normal to feature the proliferation of PPE, temperature checks at the TSA, and new cleaning procedures in cabins, leadership teams at terminals need to remember that adaptation is different from resilience.
Adaptation isn't Resilience
Adaptation is simple—follow the rules. Terminal leadership likely added thermal scanners, required masks, laid down social distancing markers on the floor, and taped off seats.
Resilience is different. Resilient businesses didn't simply change procedures, they were three steps ahead of the downturn and will be five steps ahead of the recovery.
It all comes down to the simple mantra, "if you can't clean your room, don't try to change the world."
The path to recovery is going to be a wild ride. Expect a few more false restarts followed by rising cases and consequent shutdowns. Resilience is seeing the different outcomes and staying ahead of them. Normal will come, but until then, you're going to have to weather the uncertainty—something that's not easy to do when you're trying to find out when to pull the trigger on hiring.
Building Momentum on the Road to Recovery
The recovery process is going to be unique to each airport. In fact, it's going to be unique at each terminal. International terminals are going to be a lot different than domestic, and even domestic routes are going to differ from region to region. Planning for recovery requires you to take a step back to shore up your own business. But how?
Over the past few months, we've been writing a lot on the challenges and opportunities for terminal management on the road to recovery, looking at the market trends, challenges that exist in both times of few and times of plenty, and the ways that a terminal management solution can help you deice your business processes.
Look at Your People, Processes, and Technology
People, processes, and technology each play a role in your business. Humans are absolutely vital to your company—but there are some situations in which humans are inefficient (and often quite inaccurate). Data entry is one of these areas. As much insight as a person can deliver by applying insight on a computer output, input is a different beast.
The problem is that it's not just the inefficiency, it's the repetition. People are much more valuable when they actually use their brains instead of simply using their fingers. Something we discussed in our first article in the series, manual entry was one of the biggest challenges that our client JFK Terminal One Faced—and was able to address. This helped them build resilience and ensured their billing was completed before the borders were closed.
Understand Your Challenges
For those in the terminal space, delivering support services, passenger processing, and facility management to both airlines and travelers, you're likely going to be the first to recover. But this won't be without some kind of challenge.
The problem is that you likely won't just be facing recovery challenges, you'll be facing the same challenges you faced before the virus hit. Billing will ramp up, airlines will need more services, and vendors will reopen. If your experience is anything like JFK Terminal One Group, trying to keep organized is near impossible when relying on manual processes.
But as things ramp up, you might not have the full staff available. Computation will be replaced with a cleaning crew, and without the right technology in place, the issues we discussed in our article on the four most common terminal management challenges will be even more of a concern for you.
Take Steps to Change When It's Easy
It pays to start small—and if there's one silver lining to shutdowns, it's that you have finally caught up on the backlog. As a company that's been in the ERP business for three decades, we know that it's much easier to work with clean data than disparate sources. In fact, there are few times better than now to make the move to a new business management solution.
The shock of an ERP implementation won't be as severe, the workload for your staff won't be as heavy, and this all combines to provide you with less risk and higher satisfaction.
We helped one of the busiest terminals at one of the busiest airports to make the move to better terminal management—in one of the busiest years for air travel. We got the job done with minimal risk and got them up and running in less than half a year. Get to know how we helped them deice their business processes here.
Three to Six Months Away from Terminal Velocity: MIBAR Terminal Management
Able to be implemented within three to six months, MIBAR's Terminal Management for NetSuite was specifically designed with the airport terminal manager in mind. We spent three years developing this industry-specific extension of NetSuite's ERP that delivers a unified experience for terminal managers.
This product is able to improve operational efficiency by up to 30%, incorporating contract escalation processes, third-party application extensions for workflows and various other customized elements that an airport terminal manager may need.
Get to know more about our Terminal Management Solution and contact us for a free consultation.
Giving Airport Managers the Tools They Need to Operate Efficiently and Effectively
How One Airport Terminal Weathered the Lockdown Storm
Four of the Most Common Challenges Faced by Airport Terminals
Why a Focused Solution Helps You Achieve Terminal Velocity
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text:
Private Dancer: Biopic about Black Ballerina Misty Copeland in the works
The life of African-American dance star Misty Copeland may be the subject of a new biopic.
According to Deadline.com, Copeland's rags-to-riches story is currently being developed by New Line Cinema. The film will chronicle her early years as a teen ballet prodigy who lived part-time with mother and siblings in a welfare motel and her sponsor family. However, as Copeland's star began to rise, so did a custody battle between her mother and her host family.
The film is loosely based on Copeland's NYT best-selling memoir, Life in Motion and will focus on mostly on her teen years. She is probably best known for making history as the second African-American female soloist to dance with the prestigious American Ballet Theatre. She is also the company's first African-American ballerina to dance lead in Swan Lake. Copeland has also served on President Obama's fitness council and has performed alongside music icon, Prince.
In other related news, dance legends Geoffrey Holder and Carmen De Lavallade are the subject of a new documentary available on Netflix titled, Carmen & Geoffrey.
According to Indie Wire, The film explores the couple's professional and personal lives. Holder, is an award-winning dancer, painter, actor, music composer, book author and art collector. He is also the first black man to win a Tony Award for direction and costume design for his work in the 1974 Broadway classic, The Wiz. He is also probably best-known for his role as the 7-Up man and in the 90's romantic comedy, Boomerang. His wife, Da Lavallade was the lead dancer for the Lester Horton Dance Theater and has performed alongside some of history's greats including Duke Ellington, Alvin Ailey and Josephine Baker.
Click here to see the trailer!
Photo Credits: joelmuden.com and Pintrest.com
ballerinabiopicsCarmen De LavalladedanceGeoffrey HolderMisty CopelandThe Wiz
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Box office top 20: 'Suicide Squad' dominates with $133.7M
NEW YORK (AP) — DC Comics flashed the box-office might of Marvel at the weekend box office, where its "Suicide Squad" set a record for an August debut with $133.7 million, according to final tallies Monday.
The Warner Bros. release, like March's "Batman v Superman: Dawn of Justice," was lambasted by critics. But David Ayer's antihero team-up film nevertheless became one of the summer's biggest hits.
A steep slide on Saturday, after fans flocked theaters on Thursday and Friday, however, could signal further steep declines for the $175 million film starring Will Smith, Margot Robbie and Jared Leto.
The top 20 movies at U.S. and Canadian theaters Friday through Sunday, followed by distribution studio, gross, number of theater locations, average receipts per location, total gross and number of weeks in release, as compiled Monday by comScore:
1. "Suicide Squad," Warner Bros., $133,682,248, 4,255 locations, $31,418 average, $133,682,248, 1 weeks.
2. "Jason Bourne," Universal, $22,405,125, 4,039 locations, $5,547 average, $103,111,145, 2 weeks.
3. "Bad Moms," STX Entertainment, $14,004,006, 3,215 locations, $4,356 average, $50,850,836, 2 weeks.
4. "Secret Life Of Pets, The," Universal, $11,500,590, 3,417 locations, $3,366 average, $319,519,370, 5 weeks.
5. "Star Trek Beyond," Paramount, $10,036,030, 3,263 locations, $3,076 average, $127,737,394, 3 weeks.
6. "Nine Lives," EuropaCorp, $6,249,915, 2,264 locations, $2,761 average, $6,249,915, 1 weeks.
7. "Lights Out," Warner Bros., $6,006,454, 2,581 locations, $2,327 average, $54,715,706, 3 weeks.
8. "Nerve," Lionsgate, $4,861,528, 2,538 locations, $1,915 average, $26,850,322, 2 weeks.
9. "Ghostbusters," Sony, $4,676,192, 2,545 locations, $1,837 average, $116,588,128, 4 weeks.
10. "Ice Age: Collision Course," 20th Century Fox, $4,325,094, 2,738 locations, $1,580 average, $53,564,891, 3 weeks.
11. "Finding Dory," Disney, $1,957,734, 1,122 locations, $1,745 average, $473,872,375, 8 weeks.
12. "Cafe Society," Lionsgate, $1,605,786, 631 locations, $2,545 average, $6,695,597, 4 weeks.
13. "Hillary's America: The Secret History Of," Quality Flix, $930,025, 672 locations, $1,384 average, $11,120,971, 4 weeks.
14. "Legend Of Tarzan, The," Warner Bros., $801,735, 648 locations, $1,237 average, $124,051,759, 6 weeks.
15. "Captain Fantastic," Bleecker Street, $584,171, 363 locations, $1,609 average, $3,581,232, 5 weeks.
16. "Indignation," Roadside Attractions, $420,266, 55 locations, $7,641 average, $560,512, 2 weeks.
17. "Don't Think Twice," The Film Arcade, $373,556, 57 locations, $6,554 average, $679,404, 3 weeks.
18. "Central Intelligence," Warner Bros., $371,126, 266 locations, $1,395 average, $126,088,877, 8 weeks.
19. "Hunt For The Wilderpeople," The Orchard, $335,494, 176 locations, $1,906 average, $3,469,227, 7 weeks.
20. "Absolutely Fabulous: The Movie," Fox Searchlight, $333,253, 226 locations, $1,475 average, $4,152,331, 3 weeks.
Universal and Focus are owned by NBC Universal, a unit of Comcast Corp.; Sony, Columbia, Sony Screen Gems and Sony Pictures Classics are units of Sony Corp.; Paramount is owned by Viacom Inc.; Disney, Pixar and Marvel are owned by The Walt Disney Co.; Miramax is owned by Filmyard Holdings LLC; 20th Century Fox and Fox Searchlight are owned by 21st Century Fox; Warner Bros. and New Line are units of Time Warner Inc.; MGM is owned by a group of former creditors including Highland Capital, Anchorage Advisors and Carl Icahn; Lionsgate is owned by Lions Gate Entertainment Corp.; IFC is owned by AMC Networks Inc.; Rogue is owned by Relativity Media LLC


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