An integrated view of molecular coevolution in protein-protein interactions.
Protein-protein interactions effectively mediate molecular function. They are the result of specific interactions between protein interfaces and are maintained by the action of evolutionary pressure on the regions of the interacting proteins that contribute to binding. For the most part, selection restricts amino acid replacements, accounting for the conservation of binding interfaces. However, in some cases, change in one protein will be mitigated by compensatory change in its binding partner, maintaining function in the face of evolutionary change. There have been several attempts to use correlations in sequence evolution to predict interactions of proteins. Most commonly, these approaches use the entire sequence to identify correlations and so infer probable binding. However, other factors such as shared evolutionary history and similarities in the rates of evolution confound these whole-sequence-based approaches. Here, we discuss recent work on this topic and argue that both site-specific coevolutionary change and whole-sequence evolution contribute to evolutionary signals in sets of interacting proteins. We discuss the relative effects of both types of selection and how they might be identified. This permits an integrated view of protein-protein interactions, their evolution, and coevolution.
Lovell
Simon C
SC
Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester, United Kingdom. simon.lovell@manchester.ac.uk
Robertson
David L
DL
D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding / Q000235:genetics; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D011506:Proteins