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Biochem Cell Biol. 2009 Feb;87(1):189-206. doi: 10.1139/O08-127.

Molecular dynamics of histone H1.

Author information

1
Department of Oncology, University of Alberta, University Avenue NW, Edmonton, ABT6G1Z2, Canada.

Abstract

The histone H1 family of nucleoproteins represents an important class of structural and architectural proteins that are responsible for maintaining and stabilizing higher-order chromatin structure. Essential for mammalian cell viability, they are responsible for gene-specific regulation of transcription and other DNA-dependent processes. In this review, we focus on the wealth of information gathered on the molecular kinetics of histone H1 molecules using novel imaging techniques, such as fluorescence recovery after photobleaching. These experiments have shed light on the effects of H1 phosphorylation and core histone acetylation in influencing chromatin structure and dynamics. We also delineate important concepts surrounding the C-terminal domain of H1, such as the intrinsic disorder hypothesis, and how it affects H1 function. Finally, we address the biochemical mechanisms behind low-affinity H1 binding.

PMID:
19234534
DOI:
10.1139/O08-127
[Indexed for MEDLINE]

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