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Molecular Biology and Evolution, Vol 15, 1337-1345, Copyright © 1998 by Society for Molecular Biology and Evolution

ORIGINAL ARTICLE

The correlation of protein structure and evolution of a protein-coding gene: phylogenetic inference using cytochrome oxidase III

CS Griffiths
Department of Ornithology, American Museum of Natural History, New York, New York 10024, USA. csg@amnh.org

Discriminating phylogenetic signal from noise in DNA sequence data is a difficult problem in phylogenetic inference at higher systematic levels. For protein-coding genes, noise at synonymous (silent) positions can be filtered by deleting entire codon positions or types of change at a codon position. This method is not appropriate for replacement sites, because changes at each site within a codon may not be independent. This research presents a method using information from protein structure to evaluate variation in replacement sites. Analysis of the correlation of amino acid variation with protein structure identified rapidly evolving codons in the COIII gene. In a series of phylogenetic analyses attempting to recover a known set of vertebrate relationships, downweighting these labile codons produced the most accurate results. Structural correlates of variable and invariant residues identified in this study can be used to increase the accuracy of models used for phylogenetic inference. Viewing amino acid variation within a phylogenetic framework provided insight into residue changes important in the secondary and tertiary structures of the molecule, changes that were correlated between pairs of neighboring residues or between residues in neighboring helices.
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T. R. Schmidt, W. Wu, M. Goodman, and L. I. Grossman
Evolution of Nuclear- and Mitochondrial-Encoded Subunit Interaction in Cytochrome c Oxidase
Mol. Biol. Evol., April 1, 2001; 18(4): 563 - 569.
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