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PMID: 186761 Published · ppublish English Journal Article

Studies on the interaction of H1 histone with superhelical DNA: characterization of the recognition and binding regions of H1 histones.

Nucleic acids research ·Vol. 3 ·No. 10 ·1976-10-00 ·Pages 2531-47

Singer DS, Singer MF

Abstract

The very lysine rich histone, H1, isolated from a variety of sources interacts preferentially with superhelical DNA compared to relaxed DNA duplexes. The nature of this specific interaction has been investigated by studying the ability of various purified fragments of H1 histone from calf thymus to recognize and bind superhelical DNA. The data suggest that the globular region of the H1 histone molecule (amino acid residues 72-106) is involved in the recognition of superhelical DNA. Thus, the H1 histone carboxy-terminal fragment, 72-212, resembles native H1 histone both quantitatively and qualitatively in its ability to discriminate between and bind to superhelical and relaxed DNA while the H1 histone carboxy-terminal fragment, residues 106-212, has lost this specificity, binding superhelical and relaxed DNA equally well. Furthermore, under conditions in which the globular region of the intact H1 histone has been unfolded, the molecule loses its ability to discriminate between superhelical and relaxed DNA, and binds both forms of DNA equally.

MeSH Terms
Animals Bromosuccinimide Cattle Chymotrypsin DNA, Circular/metabolism DNA, Viral/metabolism Histones/metabolism Nucleic Acid Conformation Osmolar Concentration Peptides/metabolism Protein Binding/drug effects Protein Conformation/drug effects Simian virus 40 Sodium Chloride/pharmacology Structure-Activity Relationship Thymus Gland Urea/pharmacology
Chemicals
DNA, Circular DNA, Viral Histones Peptides Sodium Chloride Urea Chymotrypsin Bromosuccinimide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Singer D S
Singer M F
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31 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/3.10.2531
Published
1976-10-00
Pages
2531-47
Language
English
Region
England
NLM ID
0411011
PMCID
PMC343111
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/3.10.2531 PMC Full Text View journal details
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