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Thermodynamic stability explains the differential evolutionary dynamics of cytochrome b and COX I in mammals
Juan Carlos Aledo1, Héctor Valverde, Manuel Ruíz-Camacho
1Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Universidad de Málaga, 29071, Málaga, Spain. caledo@uma.es
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.
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