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MBE Advance Access originally published online on September 10, 2009
Molecular Biology and Evolution 2009 26(12):2655-2659; doi:10.1093/molbev/msp211
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© The Author 2009. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Letter

Selection to Maintain Paralogous Amino Acid Differences Under the Pressure of Gene Conversion in the Heat-Shock Protein Genes in Yeast

Shohei Takuno and Hideki Innan

Graduate University for Advanced Studies, Hayama, Kanagawa, Japan

E-mail: innan_hideki{at}soken.ac.jp.

Accepted for publication September 4, 2009.

A genome scan for the signatures of selection for paralogous functional amino acid differences was performed with yeast genomes. This recently developed method makes it possible to localize the target sites of selection under the pressure of gene conversion. We found that two gene pairs have strong signatures of selection. The two pairs of duplicated genes happened to be heat shock genes (Ssa1/ Ssa2 and Ssb1/Ssb2), which have similar protein structures to each other, although the amino acid sequence identity between Ssa and Ssb is not high (~60%). Interestingly, the two gene pairs exhibit signature of selection at almost identical positions within the substrate-binding domain β. Because this domain specifies the substrate polypeptides, it is presumed that functional divergence may be advantageous in this domain. Evolutionary analysis demonstrated that the observed divergence in the two gene pairs has been maintained in many yeast species independently, suggesting long-term operation of strong selection.

Key Words: neofunctionalization • interlocus gene conversion • duplicated genes • heat-shock proteins • yeast

Kenneth Wolfe, Associate Editor


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