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Molecular Biology and Evolution, Vol 14, 1-5, Copyright © 1997 by Society for Molecular Biology and Evolution
AL Hughes
To test the hypothesis that proteins expressed in cells of the vertebrate
immune system evolve unusually rapidly, 107 orthologous immunoglobulin C2
domains were compared between human and murine rodent. The analysis showed
that the rate of nonsynonymous (amino-acid- altering) nucleotide
substitution in these domains was correlated with factors associated with
protein structure and with breadth of tissue expression, as well as with
the rate of synonymous substitution. However, when such factors were
controlled for statistically, there remained a strong positive association
between expression in the immune system and nonsynonymous rate, with the
highest rates being seen in genes expressed in the immune system only.
Certain immune system genes are known to be subject to positive selection
favoring diversity at the amino acid level; most of these genes encode
receptors that interact directly with foreign antigens. The observed
acceleration of the rate of nonsynonymous evolution in C2 domains of immune
system proteins may be explained by either (1) reduced constraint at the
amino acid level on molecules interacting with immune system receptors that
are themselves evolving rapidly due to positive diversifying selection or
(2) positive selection favoring amino acid changes correlated with changes
in the immune system receptors.
ORIGINAL ARTICLE
Rapid evolution of immunoglobulin superfamily C2 domains expressed in immune system cells
Department of Biology, Pennsylvania State University, University Park 16802, USA. austin@hugaus3.bio.psu.edu
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