Phylogenetic history and temperature adaptation contribute to structural and functional stability of proteins
Teasing apart the influences of phylogenetic history from thermal adaptation is a focal challenge in understanding the factors driving change in protein stability. This study conducted comprehensive comparative analyses between the phylogenetic relationships and functional/structural stabilities at protein and mRNA levels of cytosolic malate dehydrogenase (cMDH) orthologs of 41 marine mollusks living at widely different environmental temperatures. At the protein level, a significant negative correlation between adaptation temperature and heat-induced movements of the cMDH backbone was found. The movement fluctuation of individual residue varied similarly among cMDH orthologs. At the mRNA level, the free energy that occurs during the formation of the ensemble of mRNA secondary structure was significantly positively correlated with adaptation temperature. The fraction of guanine and cytosine increased with adaptation temperature. The proportion of variance in adaptation temperature that can be explained by the thermal stability (R2) was decreased after phylogenetic generalized least squares but was almost significant at both protein and mRNA levels (P < 0.05). Those analyses reveal the phylogenetic influence on the thermal adaptation of species. Our findings indicated that multi-level analysis of orthologous proteins should be considered alongside phylogenetic history to permit the development of a more comprehensive understanding of protein thermal adaptation.