that expression of was apparently unaffected by the growth phase of the cells in GSB or CaADH2 YNB cultures, although expression was absent under conditions of glucose excess in CaADH2 rich YPD medium, possibly indicating glucose repression of in this medium. However, CaADH2 there was no evidence for change of expression of mRNA in the three growth phases CaADH1 examined for any medium. Therefore our data would suggest that is not subject to CaADH1 glucose repression, as is the case for the ethanol utilising enzyme, ScAdh2p S. cerevisiae (Walther & Schüller, 2001, Young et al., 2008). Indeed, Siikala and colleagues have also found a remarkably high level of gene expression in cells grown in YPD containing CaADH1 C. albicans 2% glucose (Siikala et al., 2011). When expression of and was analysed using qRT-PCR under different growth CaADH1 CaADH2 conditions, there was more expression of than that of the housekeeping gene CaADH1 CaACT1 at all time points and regardless of which medium was used. This is consistent with previous observations that Adh1p is a major component of the cell proteome (Chaffin, 2008, C. albicans Kusch et al., 2008, Martínez-Gomariz et al., 2009) as well as being an immunodominant protein (Shen et al., 1991, Ishiguro et al., 1992, Swoboda et al., 1993). A decline in the level of CaADH1 expression between mid-exponential phase and stationary phase cultures was observed for cells grown in GSB media (∆Ct increase from -5.7 to -3.5; Table 3). In contrast, expression CaADH2 in GSB and YNB, as measured by qRT-PCR, was less than that of the housekeeping gene at all time points, indicating that expression of was less than that of CaACT1 CaADH2 CaADH1. Similar to expression of in GSB and YNB was also less in stationary phase CaADH1, CaADH2 cultures than in mid-exponential phase cultures. The expression of in YPD, as CaADH2 measured by qRT-PCR, was considered insignificant because the Ct values for CaADH2
that expression of CaADH2 was apparently unaffected by the growth phase of the cells in GSB or YNB cultures, although CaADH2 expression was absent under conditions of glucose excess in rich YPD medium, possibly indicating glucose repression of CaADH2 in this medium. However, there was no evidence for change of expression of CaADH1 mRNA in the three growth phases examined for any medium. Therefore our data would suggest that CaADH1 is not subject to glucose repression, as is the case for the S. cerevisiae ethanol utilising enzyme, ScAdh2p (Walther & Schüller, 2001, Young et al., 2008). Indeed, Siikala and colleagues have also found a remarkably high level of CaADH1 gene expression in C. albicans cells grown in YPD containing 2% glucose (Siikala et al., 2011). When expression of CaADH1 and CaADH2 was analysed using qRT-PCR under different growth conditions, there was more expression of CaADH1 than that of the housekeeping gene CaACT1 at all time points and regardless of which medium was used. This is consistent with previous observations that C. albicans Adh1p is a major component of the cell proteome (Chaffin, 2008, Kusch et al., 2008, Martínez-Gomariz et al., 2009) as well as being an immunodominant protein (Shen et al., 1991, Ishiguro et al., 1992, Swoboda et al., 1993). A decline in the level of CaADH1 expression between mid-exponential phase and stationary phase cultures was observed for cells grown in GSB media (∆Ct increase from -5.7 to -3.5; Table 3). In contrast, CaADH2 expression in GSB and YNB, as measured by qRT-PCR, was less than that of the housekeeping gene CaACT1 at all time points, indicating that expression of CaADH2 was less than that of CaADH1. Similar to CaADH1, expression of CaADH2 in GSB and YNB was also less in stationary phase cultures than in mid-exponential phase cultures. The expression of CaADH2 in YPD, as measured by qRT-PCR, was considered insignificant because the Ct values for CaADH2