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PMID: 8670844 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Identification of two DNA-binding sites on the globular domain of histone H5.

The EMBO journal ·Vol. 15 ·No. 13 ·1996-07-01 ·Pages 3421-9

Goytisolo FA, Gerchman SE, Yu X, Rees C, Graziano V, Ramakrishnan V, Thomas JO

Abstract

The nature of the complexes of histones H1 and H5 and their globular domains (GH1 and GH5) with DNA suggested two DNA-binding sites which are likely to be the basis of the preference of H1 and H5 for the nucleosome, compared with free DNA. More recently the X-ray and NMR structures of GH5 and GH1, respectively, have identified two basic clusters on opposite sides of the domains as candidates for these sites. Removal of the positive charge at either location by mutagenesis impairs or abolishes the ability of GH5 to assemble cooperatively in 'tramline' complexes containing two DNA duplexes, suggesting impairment or loss of its ability to bind two DNA duplexes. The mutant forms of GH5 also fail to protect the additional 20 bp of nucleosomal DNA that are characteristically protected by H1, H5 and wild-type recombinant GH5. They still bind to H1/H5-depleted chromatin, but evidently inappropriately. These results confirm the existence of, and identify the major components of, two DNA-binding sites on the globular domain of histone H5, and they strongly suggest that both binding sites are required to position the globular domain correctly on the nucleosome.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Chromatin/metabolism Circular Dichroism DNA/metabolism DNA-Binding Proteins/chemistry,metabolism Histones/chemistry,metabolism Humans Microscopy, Electron Molecular Sequence Data Mutagenesis, Site-Directed Nucleosomes/metabolism Protein Conformation Sequence Homology, Amino Acid
Chemicals
Chromatin DNA-Binding Proteins Histones Nucleosomes DNA
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Goytisolo F A
Cambridge Centre for Molecular Recognition and Department of Biochemistry, University of Cambridge, UK.
Gerchman S E
Yu X
Rees C
Graziano V
Ramakrishnan V
Thomas J O
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1996-07-01
Pages
3421-9
Language
English
Region
England
NLM ID
8208664
PMCID
PMC451906
Subset
IM
Grants
NIGMS NIH HHS · GM42796 · United States
Wellcome Trust · United Kingdom
External Links
PubMed source PMC Full Text View journal details
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