A hydrophobic ratchet entrenches molecular complexes.

ABSTRACT: Most proteins assemble into multisubunit complexes¹. The persistence of these complexes across evolutionary time is usually explained as the result of natural selection for functional properties that depend on multimerization, such as intersubunit allostery or the capacity to do mechanical work². In many complexes, however, multimerization does not enable any known function³. An alternative explanation is that multimers could become entrenched if substitutions accumulate that are neutral in multimers but deleterious in monomers; purifying selection would then prevent reversion to the unassembled form, even if assembly per se does not enhance biological function^3-7. Here we show that a hydrophobic mutational ratchet systematically entrenches molec

SUBMITTER: Hochberg GKA 

PROVIDER: S-EPMC8168016 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature