Contrasting evolutionary rates in the duplicate chaperonin genes of Mycobacterium tuberculosis and M. leprae |
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Authors: | Hughes AL |
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Institution: | Department of Biology, Pennsylvania State University, University Park 16802. |
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Abstract: | A phylogenetic analysis of chaperonin (heat shock protein 60) sequences
from prokaryotes and eukaryotes indicated that a single gene duplication
event in the common ancestor of Mycobacterium tuberculosis, M. leprae, and
Streptomyces albus gave rise to the duplicate chaperonin genes found in
these species (designated HSP65 and GroEL in the mycobacterial species).
Comparison of rates of synonymous and nonsynonymous nucleotide substitution
in different gene regions suggested that the 5' end of the HSP65 gene was
homogenized by an ancient recombination event between M. tuberculosis and
M. leprae. In S. albus, the two duplicated chaperonin genes have evolved at
essentially the same rate. In both M. tuberculosis and M. leprae, however,
the GroEL gene has evolved considerably more rapidly at nonsynonymous
nucleotide sites than has the HSP65 gene. Because this difference is not
seen at synonymous sites, it must be due to a difference in selective
constraint on the proteins encoded by the two genes, rather than to a
difference in mutation rate. The difference between GroEL and HSP65 is
striking in regions containing epitopes recognized by T cells of the
vertebrate host; in certain cross-reactive epitopes conserved across all
organisms, nonsynonymous sites in GroEL have evolved twice as fast as those
in HSP65. It is suggested that these differences are correlated with
differences in the way in which the duplicate chaperonins of M.
tuberculosis and M. leprae interact with the host immune system.
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