Acetylation-Dependent Compaction of the Histone H4 Tail Ensemble.

ABSTRACT: Acetylation of the histone H4 tail (H4Kac) has been established as a significant regulator of chromatin architecture and accessibility; however, the molecular mechanisms that underlie these observations remain elusive. Here, we characterize the ensemble features of the histone H4 tail and determine how they change following acetylation on specific sets of lysine residues. Our comprehensive account is enabled by a robust combination of experimental and computational biophysical methods that converge on molecular details including conformer size, intramolecular contacts, and secondary structure propensity. We find that acetylation significantly alters the chemical environment of basic patch residues (16-20) and leads to tail compaction that is partially mediated by transient intramolecular c

SUBMITTER: Dewing SM 

PROVIDER: S-EPMC11533190 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature