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PMID: 6449690 Published · ppublish English Journal Article

The interaction of high mobility proteins HMG14 and 17 with nucleosomes.

Nucleic acids research ·Vol. 8 ·No. 17 ·1980-09-11 ·Pages 3757-78

Sandeen G, Wood WI, Felsenfeld G

Abstract

The interaction of the high mobility group proteins, HMG14 and HMG17, with nucleosome core particles has been studied. The results show that two molecules of HMG14/17 can be bound tightly but reversibly to each core particle and that their affinity for core particles is greater than their affinity for histone-free DNA of core size. Thermal denaturation and nuclease digestion studies suggest that major sites of interaction are located near the ends of the nucleosome core DNA. When nucleosome preparations from chicken erythrocyte nuclei stripped of HMG proteins are partially titrated with HMG14/17, the nucleosome-HMG complex fraction is enriched in beta-globin gene sequences.

MeSH Terms
Animals Binding Sites Cell Membrane/metabolism Chickens Chromosomal Proteins, Non-Histone/blood DNA/blood Electrophoresis, Polyacrylamide Gel Erythrocytes/metabolism High Mobility Group Proteins Kinetics Nucleosomes/metabolism Protein Binding
Chemicals
Chromosomal Proteins, Non-Histone High Mobility Group Proteins Nucleosomes DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sandeen G
Wood W I
Felsenfeld G
References (23)
23 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/8.17.3757
Published
1980-09-11
Pages
3757-78
Language
English
Region
England
NLM ID
0411011
PMCID
PMC324193
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/8.17.3757 PMC Full Text View journal details
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