Effects of Acetylation and Phosphorylation on Subunit Interactions in Three Large Eukaryotic Complexes.

ABSTRACT: Protein post-translational modifications (PTMs) have an indispensable role in living cells as they expand chemical diversity of the proteome, providing a fine regulatory layer that can govern protein-protein interactions in changing environmental conditions. Here we investigated the effects of acetylation and phosphorylation on the stability of subunit interactions in purified Saccharomyces cerevisiae complexes, namely exosome, RNA polymerase II and proteasome. We propose a computational framework that consists of conformational sampling of the complexes by molecular dynamics simulations, followed by Gibbs energy calculation by MM/GBSA. After benchmarking against published tools such as FoldX and Mechismo, we could apply the framework for the first time on large protein assemblies w

SUBMITTER: Sostaric N 

PROVIDER: S-EPMC6283292 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature