Molecular Biology and Evolution, Vol 10, 1048-1059, Copyright © 1993 by Society for Molecular Biology and Evolution
MA Riley
To examine the hypothesis that colicin proteins are subject to
diversity-enhancing selection, we studied the rates of synonymous,
nonsynonymous, and intergenic nucleotide substitution in three pairs of
closely related colicin clusters. The results indicate that the immunity
gene and the immunity-binding domain of the colicin gene, which interact to
provide specific immunity from the lethal action of the colicin toxin,
accumulate substitutions at synonymous and nonsynonymous sites several
times more rapidly than does the remainder of the colicin cluster. We
suggest that this increased level of divergence, centered at the immunity
protein, may be the result of the combined action of recombination and
positive selection acting to increase colicin diversity in natural
populations of Escherichia coli.
ORIGINAL ARTICLE
Positive selection for colicin diversity in bacteria
Department of Biology, Yale University, New Haven, Connecticut 06511.
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