Regulation of the H4 tail binding and folding landscapes via Lys-16 acetylation.

ABSTRACT: Intrinsically disordered proteins (IDP) are a broad class of proteins with relatively flat energy landscapes showing a high level of functional promiscuity, which are frequently regulated through posttranslational covalent modifications. Histone tails, which are the terminal segments of the histone proteins, are prominent IDPs that are implicated in a variety of signaling processes, which control chromatin organization and dynamics. Although a large body of work has been done on elucidating the roles of posttranslational modifications in functional regulation of IDPs, molecular mechanisms behind the observed behaviors are not fully understood. Using extensive atomistic molecular dynamics simulations, we found in this work that H4 tail mono-acetylation at LYS-16, which is a key covalent mod

SUBMITTER: Potoyan DA 

PROVIDER: S-EPMC3497739 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature