Skip Navigation



MBE Advance Access published online on May 21, 2004
Molecular Biology and Evolution, doi:10.1093/molbev/msh161
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow Data Supplement
Right arrow Data Supplement
Right arrow All Versions of this Article:
21/8/1572    most recent
msh161v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Das, J.
Right arrow Articles by Stern, D. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Das, J.
Right arrow Articles by Stern, D. L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Accepted May 5, 2004

Original Articles

Comparison of Diverse Protein Sequences of the Nuclear-Encoded Subunits of Cytochrome C Oxidase Suggests Conservation of Structure Underlies Evolving Functional Sites

Jayatri Das 1*, Stephen T. Miller 2, David L. Stern 1

1 Department of Ecology & Evolutionary Biology, Princeton University, Princeton, NJ 08544
2 Department of Molecular Biology, Princeton University, Princeton, NJ 08544

* To whom correspondence should be addressed. E-mail: jdas{at}princeton.edu.


  Abstract

Interspecific comparisons of protein sequences can reveal regions of evolutionary conservation that are under purifying selection due to functional constraints. Interpreting these constraints requires combining evolutionary information with structural, biochemical and physiological data to understand the biological function of conserved regions. We take this integrative approach to investigate the evolution and function of the nuclear-encoded subunits of cytochrome c oxidase (COX). We find that the nuclear-encoded subunits evolved subsequent to the origin of mitochondria and the subunit composition of the holoenzyme varies across diverse taxa including animals, yeasts, and plants. By mapping conserved amino acids onto the crystal structure of bovine COX, we show that conserved residues are structurally organized into functional domains. These domains correspond to some known functional sites as well as to other uncharacterized regions. We find that amino acids important for structural stability are conserved at frequencies higher than expected within each taxon and that groups of conserved residues cluster together at distances of less that 5 Å more frequently than randomly selected residues. We therefore suggest that selection is acting to maintain the structural foundation of COX across taxa, while active sites vary or coevolve within lineages.

Key Words: cytochrome c oxidase, nuclear-encoded, evolution, structure, mitochondria


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol Biol EvolHome page
G. H. Perry, B. C. Verrelli, and A. C. Stone
Comparative Analyses Reveal a Complex History of Molecular Evolution for Human MYH16
Mol. Biol. Evol., March 1, 2005; 22(3): 379 - 382.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.