Protein Engineering vol. 9 no. 8 pp. 713-718, 1996
© 1996 Oxford University Press
RESEARCH-ARTICLE |
Expression of recombinant
Ains-crystallin and not
A-crystallin inhibits bacterial growth
1Jules Stein Eye Institute 2Brain Research Institute, UCLA School of Medicine Los Angeles, CA 90095-7008, USA
3To whom correspondence should be addressed
A-Crystallin and
Ains-crystallin are derived from the
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
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
A-crystallin and
Ains-crystallin are functionally equivalent and that the presence of the insert peptide in
AIns-crystallin is inconsequential. We report here that the independent expression of recombinant
AIns-crystallin, and not
A-crystallin, inhibits growth of the bacterial host. These observations were confirmed in co-expression 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
AIns-crystalline which causes growth inhibition. Given the prior knowledge that
A-crystallin and
AIns-crystallin differ by a peptide of 23 amino acids, these data suggest that the insert peptide in
AIns-crystallin imparts properties on this protein that are different from
A-crystallin.
Keywords: aA-crystallin/aAins-crystallin/bacterial growth/differential function/inhibition
Received November 28, 1995; revised April 5, 1996; accepted April 8, 1996.
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