Research Article

Evolution of oligomeric state through allosteric pathways that mimic ligand binding

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Science  19 Dec 2014:
Vol. 346, Issue 6216, 1254346
DOI: 10.1126/science.1254346

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Controlling the state of dynamic proteins

Small molecules that change the oligomeric state of proteins by binding to a site distant from the interface are called allosteric. They often act by taking advantage of intrinsic protein dynamics and stabilizing a particular conformation of the protein. Perica et al. show that mutations can similarly act at a distance to change protein conformation. They identified 11 mutations in an RNA- binding protein that determine whether it is stable as a dimer or a tetramer. Examination of ancestral sequences showed that the allosteric mutations are part of a downhill adaptation to lower environmental temperatures. This mechanism for modulating the oligomeric state is probably common in evolution.

Science, this issue 10.1126/science.1254346