Interaction of f1 histone with superhelical DNA.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 72 ·No. 7 ·1975-07-00 ·Pages 2597-600

Vogel T, Singer MF

Abstract

The superhelicity of double-stranded, closed circular SV40 DNA was altered by the addition of various amounts of ethidium bromide. The interaction of f1 histone with the series of molecules of various superhelicities was studied. The extent of interaction increases with increasing superhelicity regardless of whether it is of the positive or negative sense. The interaction of f1 histone with superhelical DNA is shown to be reversible.

MeSH Terms

Binding Sites DNA, Circular DNA, Viral Ethidium Histones Kinetics Macromolecular Substances Protein Binding Simian virus 40

Chemicals

DNA, Circular DNA, Viral Histones Macromolecular Substances Ethidium

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Vogel T

Singer M F

References (19)

19 references, click to expand

Thermodynamic properties of superhelical DNAs.
Biochemistry. 1975 Feb 11;14(3):527-35 PMID: 1111569
Variation of the average rotation angle of the DNA helix and the superhelical turns of covalently closed cyclic lambda DNA.
J Mol Biol. 1969 Jul 14;43(1):25-39 PMID: 4897794
Interaction of lysine-rich histones and DNA.
J Mol Biol. 1969 Aug 14;43(3):439-60 PMID: 4100471
Interactions between twisted DNAs and enzymes: the effects of superhelical turns.
J Mol Biol. 1974 Aug 25;87(4):797-816 PMID: 4279300
Supercoiling of polyoma virus DNA measured by its interaction with ethidium bromide.
J Mol Biol. 1967 Apr 14;25(1):23-30 PMID: 4291871
The interaction of closed circular DNA with intercalative dyes. I. The superhelix density of SV40 DNA in the presence and absence of dye.
J Mol Biol. 1968 Apr 14;33(1):141-71 PMID: 4296517
Sedimentation velocity behavior of closed circular SV40 DNA as a function of superhelix density, ionic strength, counterion and temperature.
J Mol Biol. 1971 Nov 28;62(1):21-38 PMID: 4333614
Occurrence and properties of a chromatin-associated F1-histone phosphokinase in mitotic Chinese hamster cells.
Biochemistry. 1972 Dec 5;11(25):4817-26 PMID: 4347703
Control of cell division by very lysine rich histone (F1) phosphorylation.
Nature. 1974 Feb 1;247(5439):257-61 PMID: 4361936
Effect of circularity and superhelicity on transcription from bacteriophagelambda DNA.
Proc Natl Acad Sci U S A. 1973 Nov;70(11):3077-81 PMID: 4594034
Measurements of unwinding of lac operator by repressor.
Nature. 1974 Sep 20;251(5472):247-9 PMID: 4609322
A model for particulate structure in chromatin.
Nucleic Acids Res. 1974 Nov;1(11):1579-86 PMID: 10793713
Degree of superhelicity of covalently closed cyclic DNA's from Escherichia coli.
J Mol Biol. 1969 Jul 28;43(2):263-72 PMID: 4979717
The role of histones in the maintenance of chromatin structure.
Proc Natl Acad Sci U S A. 1965 Oct;54(4):1204-12 PMID: 5219825
A fluorescent complex between ethidium bromide and nucleic acids. Physical-chemical characterization.
J Mol Biol. 1967 Jul 14;27(1):87-106 PMID: 6033613
Selective retention of double-stranded circular deoxyribonucleic acid by membrane filtration.
Biochemistry. 1973 Jul 3;12(14):2755-8 PMID: 4711478
Chromatin structure; oligomers of the histones.
Science. 1974 May 24;184(4139):865-8 PMID: 4825888
Chromatin structure: a repeating unit of histones and DNA.
Science. 1974 May 24;184(4139):868-71 PMID: 4825889
The interaction of histones with simian virus 40 supercoiled circular deoxyribonucleic acid in vitro.
J Biol Chem. 1975 Jan 25;250(2):796-8 PMID: 163237

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.72.7.2597

Published

1975-07-00

Pages

2597-600

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC432816

Subset

External Links

PubMed source DOI: 10.1073/pnas.72.7.2597 PMC Full Text View journal details

Analysis Services

Interaction of f1 histone with superhelical DNA.

Contact

WeChat Official Account