Extreme primary and secondary protein structure variability in the chimeric male-transmitted cytochrome c oxidase subunit II protein in freshwater mussels: Evidence for an elevated amino acid substitution rate in the face of domain-specific purifying selection

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Research article

Eric G Chapman¹ , Helen Piontkivska¹ , Jennifer M Walker² , Donald T Stewart³ , Jason P Curole⁴ and Walter R Hoeh¹

¹Department of Biological Sciences, Kent State University, Kent, OH 44242, USA

²Department of Biological Sciences, The University of Southern Mississippi, Long Beach, MS 39560, USA

³Acadia University, Wolfville, Nova Scotia, B4P 2R6, Canada

⁴University of Southern California, Los Angeles, CA 90089, USA

author email corresponding author email

BMC Evolutionary Biology 2008, 8:165doi:10.1186/1471-2148-8-165


Published:	31 May 2008

Additional file 1:

Amino acid sequences deduced from the complete Mcox2 extension nucleotide sequences of the 21 species used in this study.

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Additional file 2:

Pairwise amino acid and nucleotide distances (based on PC and TN models, respectively).

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Additional file 3:

Codeml log-likelihood values and parameter estimates for four models applied to the M and F COX2+COX1 regions.

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Additional file 4:

Summary of TreeSAAP output showing the 31 amino acid properties of MCOX2h+MCOX1, MCOX2e and FCOX2+FCOX1.

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