Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release

The histone chaperone nucleoplasmin (Npm) stores histones H2A/H2B in the egg and embryo. Here, the authors use NMR to show that Npm’s intrinsically disordered tail domain controls histone binding at an acidic stretch, which is autoregulated through direct competition with its basic C-terminus.

Bibliographic Details
Main Authors: Christopher Warren, Tsutomu Matsui, Jerome M. Karp, Takashi Onikubo, Sean Cahill, Michael Brenowitz, David Cowburn, Mark Girvin, David Shechter
Format: Article
Language:English
Published: Nature Publishing Group 2017-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02308-3