Thermodynamic Stability Explains the Differential Evolutionary Dynamics of Cytochrome b and COX I in Mammals

被引：7

作者：

Carlos Aledo, Juan ^{[1
]}

Valverde, Hector ^{[1
]}

Ruiz-Camacho, Manuel ^{[2
]}

机构：

[1] Univ Malaga, Fac Ciencias, Dept Biol Mol & Bioquim, E-29071 Malaga, Spain

[2] Univ Malaga, Fac Ciencias, Dept Estadist & Invest Operat, E-29071 Malaga, Spain

来源：

JOURNAL OF MOLECULAR EVOLUTION | 2012年 / 74卷 / 1-2期

关键词：

COX I; Cytochrome b; Evolvability; mtDNA; Natural selection; Protein evolution; PROTEIN EVOLUTION; STRUCTURAL DETERMINANTS; MITOCHONDRIAL-DNA; MUTATIONS; SELECTION; SURFACE; SYSTEM; GENES; YEAST; BIAS;

D O I：

10.1007/s00239-012-9489-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

By using a combination of evolutionary and structural data from 231 species, we have addressed the relationship between evolution and structural features of cytochrome b and COX I, two mtDNA-encoded proteins. The interior of cytochrome b, in contrast to that of COX I, exhibits a remarkable tolerance to changes. The higher evolvability of cytochrome b contrasts with the lower rate of synonymous substitutions of its gene when compared to that of COX I, suggesting that the latter is subjected to a stronger purifying selection. We present evidences that the stability effect of mutations (Delta Delta G) may be behind these differential behaviour.

引用

页码：69 / 80

页数：12

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