Abstract
CspA was originally found as the major cold-shock protein in Escherichia coli, consisting of 70-amino-acid residues. It forms a beta-barrel structure with five anti-parallel beta-strands and functions as an RNA chaperone. Its dramatic but transient induction upon cold shock is regulated at the level of transcription, mRNA stability and translation. Surprisingly, E. coli contains a large CspA family, consisting of nine genes from cspA to cspI. Phylogenetic analysis of these gene products and the cold-shock domain of human YB-1 protein reveals that there are two major branches in the evolution of CspA homologues: one branch for CspF and CspH, and another for all the other known CspA homologues from both prokaryotes and eukaryotes. The locations of these genes on the E. coli chromosome suggest that the large CspA family probably resulted from a number of gene duplications and, after subsequent adaptation, resulted in specific groups of genes that respond to different environmental stresses; for example, cspA, cspB and cspG for cold-shock stress and cspD for nutritional deprivation. The E. coli CspA family will be discussed in terms of their structures and functions, and their gene structures and regulation.
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