Dynamic binding of histone H1 to chromatin in living cells

Tom Misteli (), Akash Gunjan, Robert Hock, Michael Bustin and David T. Brown
Additional contact information
Tom Misteli: National Cancer Institute, NIH
Akash Gunjan: University of Mississippi Medical Center
Robert Hock: University of Wuerzburg, Biocenter
Michael Bustin: National Cancer Institute, NIH, Laboratory of Molecular Biology
David T. Brown: University of Mississippi Medical Center

Nature, 2000, vol. 408, issue 6814, 877-881

Abstract: 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.

Date: 2000
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DOI: 10.1038/35048610

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