Progressive Phosphorylation Modulates the Self-Association of a Variably Modified Histone H3 Peptide.

ABSTRACT: Protein phosphorylation is a key regulatory mechanism in eukaryotic cells. In the intrinsically disordered histone tails, phosphorylation is often a part of combinatorial post-translational modifications and an integral part of the "histone code" that regulates gene expression. Here, we study the association between two histone H3 tail peptides modified to different degrees, using fully atomistic molecular dynamics simulations. Assuming that the initial conformations are either α-helical or fully extended, we compare the propensity of the two peptides to associate with one another when both are unmodified, one modified and the other unmodified, or both modified. The simulations lead to the identification of distinct inter- and intramolecular interactions in the peptide dimer, highlighting

SUBMITTER: Papamokos GV 

PROVIDER: S-EPMC8226166 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature