Expression of recombinant alpha Ains-crystallin and not alpha A-crystallin inhibits bacterial growth.

alpha A-Crystallin and alpha Ains-crystallin are derived from the alpha A-crystallin gene via alternative splicing. They are identical except for the presence of a polypeptide, 23 amino acids long, encoded by the 'insert' exon. Evolutionary logic would suggest that the insertion of a 23 amino acid peptide in the middle of alpha A-crystallin, a protein evolving more slowly than either histone H1, cytochrome c or hemoglobin, would lead to appreciable structural and functional changes. However, based on physico-chemical studies, it is presently believed that alpha A-crystallin and alpha Ains-crystallin are functionally equivalent and that the presence of the 'insert' peptide in alpha Ains-crystallin is inconsequential. We report here that the independent expression of recombinant alpha Ains-crystallin, and not alpha A-crystallin, inhibits growth of the bacterial host. These observations were confirmed in coexpression experiments, wherein both the proteins were expressed in the same cell. Interestingly, growth inhibition is reversible. Importantly, the data demonstrate that it is catalytic amounts and not the gross accumulation of alpha Ains-crystallin which causes growth inhibition. Given the prior knowledge that alpha A-crystallin and alpha Ains-crystallin differ by a peptide of 23 amino acids, these data suggest that the "insert peptide' in alpha Ains-crystallin imparts properties on this protein that are different from alpha A-crystallin.