Towards a mechanism for histone chaperones.
Histone chaperones can be broadly defined as histone-binding proteins that influence chromatin dynamics in an ATP-independent manner. Their existence reflects the importance of chromatin homeostasis and the unique and unusual biochemistry of the histone proteins. Histone supply and demand at chromatin is regulated by a network of structurally and functionally diverse histone chaperones. At the core of this network is a mechanistic variability that is only beginning to be appreciated. In this review, we highlight the challenges in determining histone chaperone mechanism and discuss possible mechanisms in the context of nucleosome thermodynamics. We discuss how histone chaperones prevent promiscuous histone interactions, and consider if this activity represents the full extent of histone chaperone function in governing chromatin dynamics. This article is part of a Special Issue entitled: Histone chaperones and Chromatin assembly.
Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, Box 374, 1230 York Ave, New York, NY 10065, USA.
Simon J
SJ
Elsässer
Howard Hughes Medical Institute, Colorado State University, Fort Collins CO 80523, USA; Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins CO 80523, USA.
Sheena
S
D'Arcy
D000818:Animals; D042002:Chromatin Assembly and Disassembly / Q000502:physiology; D056488:Histone Chaperones / Q000737:chemistry / Q000502:physiology*; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism
D056488:Histone Chaperones; D006657:Histones; D009707:Nucleosomes