@article {13648,
	title = {Rapid nonsynonymous evolution of the iron-sulfur protein in anthropoid primates},
	journal = {J Bioenerg Biomembr},
	volume = {37},
	number = {1},
	year = {2005},
	note = {<p>J Bioenerg Biomembr. 2005 Feb;37(1):35-41.</p>},
	month = {Feb},
	pages = {35-41},
	type = {Comparative StudyResearch Support, N.I.H., ExtramuralResearch Support, U.S. Gov{\textquoteright}t, Non-P.H.S.Research Support, U.S. Gov{\textquoteright}t, P.H.S.},
	edition = {2005/05/21},
	abstract = {<p>Cytochrome c (CYC) and 9 of the 13 subunits of cytochrome c oxidase (complex IV; COX) were previously shown to have accelerated rates of nonsynonymous substitution in anthropoid primates. Cytochrome b, the mtDNA encoded subunit of ubiquinol-cytochrome c reductase (complex III), also showed an accelerated nonsynonymous substitution rate in anthropoid primates but rate information about the nuclear encoded subunits of complex III has been lacking. We now report that phylogenetic and relative rates analysis of a nuclear encoded catalytically active subunit of complex III, the iron-sulfur protein (ISP), shows an accelerated rate of amino acid replacement similar to cytochrome b. Because both ISP and subunit 9, whose function is not directly related to electron transport, are produced by cleavage into two subunits of the initial translation product of a single gene, it is probable that these two subunits of complex III have essentially identical underlying rates of mutation. Nevertheless, we find that the catalytically active ISP has an accelerated rate of amino acid replacement in anthropoid primates whereas the catalytically inactive subunit 9 does not.</p>},
	keywords = {*Evolution, Amino Acid Sequence, Amino Acid Substitution, Animals, Humans, Iron-Sulfur Proteins/chemistry/*genetics, Lemur, Liver/metabolism, Molecular, Phylogeny, Primates/classification/*genetics, Species Specificity},
	isbn = {0145-479X (Print)0145-47},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/15906147},
	author = {Doan, J. W. and Schmidt, T. R. and Wildman, D. E. and Goodman, M. and Weiss, M. L. and Grossman, L. I.}
}
