Modulation of histone tail electrostatic potentials in nucleosome core particles by acetylation and PARylation.

ABSTRACT: Cellular DNA is wrapped about an octamer composed of four histone proteins forming the fundamental unit of chromatin structure, the nucleosome core particle (NCP). The intrinsically disordered tails of the histones serve as scaffolds for binding an array of proteins that regulate the fidelity of the genome and gene expression. A variety of posttranslational modifications (PTMs) on the tails have been characterized, including some that alter their overall charge; however, per-residue changes in tail electrostatic potentials for different PTMs have not been reported. Here, using a solution NMR approach in which enhancements of transverse relaxation rates of tail amide and methyl group protons are quantified through the addition of paramagnetic cosolutes, we examine how acetylation and PARyla

SUBMITTER: Bolik-Coulon N 

PROVIDER: S-EPMC12318224 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature