Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 72 ·No. 9 ·1975-09-00 ·Pages 3428-32

Rouvière-Yaniv J, Gros F

Abstract

A low-molecular-weight (7000), heat-stable protein--HU--that stimulates transcription of bacteriophage lambda DNA by E. coli RNA polymerase was purified from E. coli extracts using affinity chromatography on DNA-cellulose. HU binds to native DNA, resulting in an apparent thickening of the DNA chains as revealed by electron microscopy. Contrary to DNA unwinding proteins, it causes no destabilization of the double helix. HU differs from previously described transcription factors (H1, D, etc.) and from the low-molecular-weight omega subunit of the RNA polymerase. By its amino-acid composition and characteristics, HU displays an interesting resemblance to some eukaryotic histones, such as H2B and H1.

MeSH Terms

Amino Acids/analysis Bacterial Proteins/isolation & purification,metabolism Binding Sites Coliphages DNA, Bacterial/metabolism DNA, Viral/metabolism Escherichia coli/metabolism Hot Temperature Molecular Weight Transcription, Genetic/drug effects

Chemicals

Amino Acids Bacterial Proteins DNA, Bacterial DNA, Viral

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Rouvière-Yaniv J

Gros F

References (21)

21 references, click to expand

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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.72.9.3428

Published

1975-09-00

Pages

3428-32

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC433007

Subset

External Links

PubMed source DOI: 10.1073/pnas.72.9.3428 PMC Full Text View journal details

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Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli.

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