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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.
- Source :
- Journal of Biological Chemistry; October 1996, Vol. 271 Issue: 42 p25817-22, 6p
- Publication Year :
- 1996
-
Abstract
- 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 H1(0), 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.
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Volume :
- 271
- Issue :
- 42
- Database :
- Supplemental Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Periodical
- Accession number :
- ejs7180471