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Volume 271, Number 42, Issue of October 18, 1996 pp. 25817-25822
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Putative DNA Binding Surface in the Globular Domain of a Linker Histone Is Not Essential for Specific Binding to the Nucleosome

(Received for publication, February 23, 1996, and in revised form, July 12, 1996)

From the Department of Biochemistry, University of Rochester Medical Center, Rochester, New York 14642 and the ^§ Laboratory of Molecular Embryology, NICHD, National Institutes of Health, Bethesda, Maryland 20892

A fundamental step in the assembly of native chromatin is the specific recognition and binding of linker histones to the nucleoprotein subunit known as the nucleosome. A first step in defining this important interaction is the determination of residues within linker histones that are important for the structure-specific recognition of the nucleosome core. By combining in vitro assays for the native binding activity of linker histones and site-directed mutagenesis, we have examined a cluster of basic residues within the globular domain of H1⁰, a somatic linker histone variant from Xenopus laevis. We show that these residues, which comprise a putative DNA binding surface within the globular domain, do not play an essential role in the structure-specific binding of a linker histone to the nucleosome.

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