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Updated: May 23, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
Published on: December 29, 2021
Histone transfer among chaperones
Wallace H Liu1, Mair E A Churchill
1Department of Pharmacology, University of Colorado School of Medicine, Mail Stop 8303, PO Box 6511, Aurora, CO 80045, USA.
Abstract:
The eukaryotic processes of nucleosome assembly and disassembly govern chromatin dynamics, in which histones exchange in a highly regulated manner to promote genome accessibility for all DNA-dependent processes. This regulation is partly carried out by histone chaperones, which serve multifaceted roles in co-ordinating the interactions of histone proteins with modification enzymes, nucleosome remodellers, other histone chaperones and nucleosomal DNA. The molecular details of the processes by which histone chaperones promote delivery of histones among their many functional partners are still largely undefined, but promise to offer insights into epigenome maintenance. In the present paper, we review recent findings on the histone chaperone interactions that guide the assembly of histones H3 and H4 into chromatin. This evidence supports the concepts of histone post-translational modifications and specific histone chaperone interactions as guiding principles for histone H3/H4 transactions during chromatin assembly.
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