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PMID: 6306467 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Escherichia coli single-strand binding protein stabilizes specific denatured sites in superhelical DNA.

Nature ·Vol. 303 ·No. 5920 ·1983-06-30 ·Pages 770-4

Glikin GC, Gargiulo G, Rena-Descalzi L, Worcel A

Abstract

Escherichia coli single-strand binding protein relaxes supercoiled DNA molecules containing the Drosophila melanogaster histone gene repeat unit, by stabilizing denaturation bubbles that map near the boundaries of the genes, at sites that in native chromatin have been shown to be hypersensitive to nucleases. A similar process may contribute to the propagation of such hypersensitive sites after their induction on the activation of gene expression.

MeSH Terms
Bacterial Proteins/pharmacology DNA Helicases/pharmacology DNA, Superhelical/genetics DNA-Binding Proteins Drosophila melanogaster/genetics Escherichia coli/genetics,metabolism Histones/genetics Nucleic Acid Denaturation
Chemicals
Bacterial Proteins DNA, Superhelical DNA-Binding Proteins Histones DNA Helicases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Glikin G C
Gargiulo G
Rena-Descalzi L
Worcel A
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1983-06-30
Pages
770-4
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
PHS HHS · 30332 · United States
PHS HHS · 30339 · United States
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