Molecular Biology and Evolution, Vol 10, 103-126, Copyright © 1993 by Society for Molecular Biology and Evolution
WW de Jong, JA Leunissen and CE Voorter
The common characteristic of the alpha-crystallin/small heat-shock protein
family is the presence of a conserved homologous sequence of 90- 100
residues. Apart from the vertebrate lens proteins--alpha A- and alpha
B-crystallin--and the ubiquitous group of 15-30-kDa heat-shock proteins,
this family also includes two mycobacterial surface antigens and a major
egg antigen of Schistosoma mansoni. Multiple small heat- shock proteins are
especially present in higher plants, where they can be distinguished in at
least two classes of cytoplasmic proteins and a chloroplast-located class.
The alpha-crystallins have recently been found in many tissues outside the
lens, and alpha B-crystallin, in particular, behaves in many respects like
a small heat-shock protein. The homologous sequences constitute the
C-terminal halves of the proteins and probably represent a structural
domain with a more variable C-terminal extension. These domains must be
responsible for the common structural and functional properties of this
protein family. Analysis of the phylogenetic tree and comparison of the
biological properties of the various proteins in this family suggest the
following scenario for its evolution: The primordial role of the small
heat-shock protein family must have been to cope with the destabilizing
effects of stressful conditions on cellular integrity. The
alpha-crystallin-like domain appears to be very stable, which makes it
suitable both as a surface antigen in parasitic organisms and as a
long-living lens protein in vertebrates. It has recently been demonstrated
that, like the other heat-shock proteins, the alpha-crystallins and small
heat- shock proteins function as molecular chaperones, preventing undesired
protein-protein interactions and assisting in refolding of denatured
proteins. Many of the small heat-shock proteins are differentially
expressed during normal development, and there is good evidence that they
are involved in cytomorphological reorganizations and in degenerative
diseases. In conjunction with the stabilizing, thermoprotective role of
alpha-crystallins and small heat-shock proteins, they may also be involved
in signal transduction. The reversible phosphorylation of these proteins
appears to be important in this respect.
REVIEW ARTICLE
Evolution of the alpha-crystallin/small heat-shock protein family
Department of Biochemistry, University of Nijmegen, The Netherlands.
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