<p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</p> <p>The Elip (early light-inducible protein) family in pro- and eukaryotic photosynthetic organisms consists of more than 100 different stress proteins. These proteins
accumulate in photosynthetic membranes in response to light stress and have
photoprotective functions. At the amino acid level, members of the Elip family are
closely related to light-harvesting chlorophyll <italic>a/b</italic>-binding (Cab) antenna proteins
of photosystem I and II, present in higher plants and some algae. Based on their
predicted secondary structure, members of the Elip family are divided into three
groups: (a) one-helix Hlips (high light-induced proteins), also called Scps (small
Cab-like proteins) or Ohps (one-helix proteins); (b) two-helix Seps (stress-enhanced
proteins); and (c) three-helix Elips and related proteins. Despite having different
physiological functions it is believed that eukaryotic three-helix Cab proteins evolved
from the prokaryotic Hlips through a series of duplications and fusions. In this
review we analyse the occurrence of Elip family members in various photosynthetic
prokaryotic and eukaryotic organisms and discuss their evolutionary relationship
with Cab proteins.</p>
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Comp Funct Genomics. 2002 Dec; 3(6):504-510