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Determinants of histone H1 mobility and chromatin binding in living cells

Nature Structural & Molecular Biology volume 13, pages 305–310 (2006)Cite this article

Abstract

The dynamic interaction of chromatin-binding proteins with their nucleosome binding sites is an important element in regulating the structure and function of chromatin in living cells. Here we review the major factors regulating the intranuclear mobility and chromatin binding of the linker histone H1, the most abundant family of nucleosome-binding proteins. The information available reveals that multiple and diverse factors modulate the interaction of H1 with chromatin at both a local and global level. This multifaceted mode of modulating the interaction of H1 with nucleosomes is part of the mechanism that regulates the dynamics of the chromatin fiber in living cells.

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Figure 1: Analysis of protein dynamics in living cells by FRAP.
Figure 2: Structural features of H1 variants.
Figure 3: Dynamic binding of H1 to chromatin.
Figure 4: Determinants of H1-nucleosome interactions.

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Acknowledgements

This work was supported by the Center for Cancer Research, NCI, through the Intramural Research Program of the US National Institutes of Health. We thank M. Wittenberger, G. Gerlitz and D. Landsman for helpful comments on the manuscript and T. Misteli for critical comments, for numerous discussions on the topic and for providing access to his manuscripts before their publication.

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  1. Frédéric Catez

    Present address: Centre de Genetique Moleculaire et Cellulaire, UMR5534 Centre National de la Recherche Scientifique/Université Claude Bernard Lyon, 69622, Villeurbanne, France

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  1. Protein Section, Laboratory of Metabolism, National Cancer Institute (NCI), US National Institutes of Health, Bethesda, 20892, Maryland, USA

    Frédéric Catez, Tetsuya Ueda & Michael Bustin

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Correspondence to Michael Bustin.

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Catez, F., Ueda, T. & Bustin, M. Determinants of histone H1 mobility and chromatin binding in living cells. Nat Struct Mol Biol 13, 305–310 (2006). https://doi.org/10.1038/nsmb1077

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