Structural variability of multifunctional proteins indicates frequent stochastic evolution of protein oligomers.

ABSTRACT: Recently, it has been suggested that the evolution of many protein homomer complexes follows a neutral pattern, with little effect on their biochemical function. One of the strongest arguments in support of this hypothesis is the observation that homologous enzymes with the same catalytic function can have different quaternary structures in various species. However, in the case of proteins with multiple functions ("moonlighting" proteins), this pattern can also have an adaptive explanation if quaternary structure is responsible for their variable, non-canonical functions. To test whether moonlighting can be responsible for the variability of quaternary structure, here we examine the opposite of the "same function-multiple structures" pattern, and test whether orthogroups of moonlighting (m

SUBMITTER: Abrusan G 

PROVIDER: S-EPMC12749353 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature