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J. Biol. Chem., Vol. 279, Issue 19, 20028-20034, May 7, 2004

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The C-terminal Domain Is the Primary Determinant of Histone H1 Binding to Chromatin in Vivo^*

Michael J. Hendzel, Melody A. Lever, Ellen Crawford, and John P. H. Th'ng¶||

From the Cross Cancer Institute and Department of Oncology, University of Alberta, Edmonton, Alberta T6G 1Z2, and ^¶Northwestern Ontario Regional Cancer Center, Thunder Bay, Ontario P7B 6V4, Canada

We have used a combination of kinetic measurements and targeted mutations to show that the C-terminal domain is required for high-affinity binding of histone H1 to chromatin, and phosphorylations can disrupt binding by affecting the secondary structure of the C terminus. By measuring the fluorescence recovery after photo-bleaching profiles of green fluorescent protein-histone H1 proteins in living cells, we find that the deletion of the N terminus only modestly reduces binding affinity. Deletion of the C terminus, however, almost completely eliminates histone H1.1 binding. Specific mutations of the C-terminal domain identified Thr-152 and Ser-183 as novel regulatory switches that control the binding of histone H1.1 in vivo. It is remarkable that the single amino acid substitution of Thr-152 with glutamic acid was almost as effective as the truncation of the C terminus to amino acid 151 in destabilizing histone H1.1 binding in vivo. We found that modifications to the C terminus can affect histone H1 binding dramatically but have little or no influence on the charge distribution or the overall net charge of this domain. A comparison of individual point mutations and deletion mutants, when reviewed collectively, cannot be reconciled with simple charge-dependent mechanisms of C-terminal domain function of linker histones.

Received for publication, January 5, 2004 , and in revised form, February 23, 2004.

^* This work was supported by a Canadian Institutes of Health Research project grant (to J. T. and M. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Scholar of the Alberta Heritage Foundation for Medical Research and the Canadian Institutes of Health Research.

^|| To whom correspondence should be addressed: 980 Oliver Rd., Thunder Bay, Ontario P7B 6V4, Canada. Tel.: 807-684-7245; Fax: 807-684-5803; E-mail: thngj{at}tbh.net.

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