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Published 30 September 2002. doi:10.1083/jcb.200202131
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© The Rockefeller University Press, 0021-9525/2002/9/1161 $5.00
The Journal of Cell Biology, Volume 158, Number 7, September 30, 2002 1161-1170

Article

 Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin

Yali Dou, Josephine Bowen, Yifan Liu and Martin A. Gorovsky

Department of Biology, University of Rochester, Rochester, NY 14627

Address correspondence to Martin A. Gorovsky, Dept. of Biology, University of Rochester, Rochester, NY 14627. Tel.: (585) 275-6988. Fax: (585) 275-2070. E-mail: goro{at}mail.rochester.edu

In Tetrahymena cells, phosphorylation of linker histone H1 regulates transcription of specific genes. Phosphorylation acts by creating a localized negative charge patch and phenocopies the loss of H1 from chromatin, suggesting that it affects transcription by regulating the dissociation of H1 from chromatin. To test this hypothesis, we used FRAP of GFP-tagged H1 to analyze the effects of mutations that either eliminate or mimic phosphorylation on the binding of H1 to chromatin both in vivo and in vitro. We demonstrate that phosphorylation can increase the rate of dissociation of H1 from chromatin, providing a mechanism by which it can affect H1 function in vivo. We also demonstrate a previously undescribed ATP-dependent process that has a global effect on the dynamic binding of linker histone to chromatin.

Key Words: H1; phosphorylation; ATP remodeling; FRAP; Tetrahymena


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