title: Thermodynamic stability explains the differential evolutionary dynamics of cytochrome b and COX I in mammals.
abstract: 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 (ΔΔG) may be behind these differential behaviour.
authors.affiliation: Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Universidad de Málaga, 29071, Málaga, Spain. caledo@uma.es
authors.forename: Juan Carlos
authors.initials: JC
authors.lastname: Aledo
authors.forename: Héctor
authors.initials: H
authors.lastname: Valverde
authors.forename: Manuel
authors.initials: M
authors.lastname: Ruíz-Camacho
mesh_terms: D000818:Animals; D045303:Cytochromes b / Q000235:genetics*; D003576:Electron Transport Complex IV / Q000235:genetics*; D019277:Entropy; D019143:Evolution, Molecular; D008322:Mammals / Q000235:genetics*; D009154:Mutation / Q000235:genetics; D010802:Phylogeny; D055550:Protein Stability; D012641:Selection, Genetic; D013045:Species Specificity
chemical_list: D045303:Cytochromes b; D003576:Electron Transport Complex IV