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Dynamic binding of histone H1 to chromatin in living cells

Nature volume 408, pages 877–881 (2000)Cite this article

Abstract

The linker histone H1 is believed to be involved in chromatin organization by stabilizing higher-order chromatin structure1,2,3. Histone H1 is generally viewed as a repressor of transcription as it prevents the access of transcription factors and chromatin remodelling complexes to DNA4,5,6. Determining the binding properties of histone H1 to chromatin in vivo is central to understanding how it exerts these functions. We have used photobleaching techniques to measure the dynamic binding of histone H1–GFP to unperturbed chromatin in living cells. Here we show that almost the entire population of H1–GFP is bound to chromatin at any one time; however, H1–GFP is exchanged continuously between chromatin regions. The residence time of H1–GFP on chromatin between exchange events is several minutes in both euchromatin and heterochromatin. In addition to the mobile fraction, we detected a kinetically distinct, less mobile fraction. After hyperacetylation of core histones, the residence time of H1–GFP is reduced, suggesting a higher rate of exchange upon chromatin remodelling. These results support a model in which linker histones bind dynamically to chromatin in a stop-and-go mode.

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Figure 1: Properties of H1–GFP proteins.
Figure 2: FRAP analysis of H1–GFP.
Figure 3: FRAP on H1–GFP in heterochromatin or euchromatin.
Figure 4: FRAP on H1–GFP in heterochromatin or euchromatin after TSA treatment.

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Acknowledgements

We thank D. Sittman for valuable discussion, S. Leuba for critical comments on the manuscript and E. Minc for providing HP1 antibodies.

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Author notes

  1. Akash Gunjan

    Present address: Imperial Cancer Research Fund, Potters Bar, EN6 3LD, UK

Authors and Affiliations

  1. National Cancer Institute, NIH, Bethesda, 20892, Maryland, USA

    Tom Misteli

  2. University of Mississippi Medical Center, Jackson, 39216, Mississippi, USA

    Akash Gunjan & David T. Brown

  3. University of Wuerzburg, Biocenter , Germany

    Robert Hock

  4. National Cancer Institute, NIH, Laboratory of Molecular Biology, Bethesda, D 20892, Maryland, USA

    Michael Bustin

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  1. Tom Misteli
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Correspondence to Tom Misteli.

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Misteli, T., Gunjan, A., Hock, R. et al. Dynamic binding of histone H1 to chromatin in living cells. Nature 408, 877–881 (2000). https://doi.org/10.1038/35048610

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