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PMID: 6379600 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro.

Nucleic acids research ·Vol. 12 ·No. 13 ·1984-07-11 ·Pages 5321-40

Spassky A, Rimsky S, Garreau H, Buc H

Abstract

We characterize a component of the E. coli bacterial nucleoid H1a, which accumulates in stationary phase. This protein, identical with the major component of a plasmid-protein complex previously isolated in our laboratory, has a pI close to 7.5. Acrylamide gel electrophoresis and sedimentation in sucrose gradient have shown that the protein H1a induces significant compaction into DNA. This compaction is equivalent to that observed in nucleosome core although it introduces only a slight change in linking number. In addition, the structural change induced in the lactose L8UV5 promoter by H1a results in the decrease in the kinetic of formation of the open complex with RNA polymerase.

MeSH Terms
Bacterial Proteins/isolation & purification DNA, Bacterial/isolation & purification,metabolism DNA-Binding Proteins/isolation & purification,metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli/genetics,metabolism Kinetics Operon Plasmids Transcription, Genetic
Chemicals
Bacterial Proteins DNA, Bacterial DNA-Binding Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Spassky A
Rimsky S
Garreau H
Buc H
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49 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/12.13.5321
Published
1984-07-11
Pages
5321-40
Language
English
Region
England
NLM ID
0411011
PMCID
PMC318922
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/12.13.5321 PMC Full Text View journal details
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