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PMID: 7453800 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The structure of histone H1 and its location in chromatin.

Nature ·Vol. 288 ·No. 5792 ·1980-12-25 ·Pages 675-9

Allan J, Hartman PG, Crane-Robinson C, Aviles FX

Abstract

On the basis of their primary structure, the lysine-rich histones are a unified family of proteins. Each has an amino acid chain which falls into three distinct domains. Only the central domain (approximately 80 residues) is in a folded conformation. It is protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation. Without the flanking domains it is able to close two full turns of DNA in the nucleosome and can thus locate the H1 molecule.

MeSH Terms
Amino Acid Sequence Animals Cattle Chromatin/ultrastructure DNA/metabolism Histones Nucleic Acid Conformation Nucleosomes/ultrastructure Protein Binding Protein Conformation Trypsin/metabolism
Chemicals
Chromatin Histones Nucleosomes DNA Trypsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Allan J
Hartman P G
Crane-Robinson C
Aviles F X
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1980-12-25
Pages
675-9
Language
English
Region
England
NLM ID
0410462
Subset
IM
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