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PMID: 2682620 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Lon-dependent regulation of the DNA binding protein HU in Escherichia coli.

Bonnefoy E, Almeida A, Rouviere-Yaniv J

Abstract

HU, the major DNA binding protein of Escherichia coli, exists in solution as a heterodimer composed of two highly homologous subunits: HU1, encoded by hupB; HU2, encoded by hupA. The purification of the HU protein from hupA- or hupB- bacteria showed that the hupB mutant strains synthesize normal amounts of the HU2 subunit (which corresponds to 60% of the total HU present in wild-type cells). On the contrary, the amount of HU1 present in hupA mutant strains corresponds to only 6% of the total HU present in wild-type cells. We showed by fusions of the hupB and hupA promoters to the malPQ operon that the absence of one subunit has no major effect on the transcription rate of the gene encoding the other subunit. Analysis of the stability of the HU1 and HU2 subunits, using pulse-chase labeling experiments, showed that the HU1 subunit is degraded specifically in the absence of the HU2 subunit and, moreover, that this degradation is dependent on the presence of the Lon protease.

MeSH Terms
ATP-Dependent Proteases Bacterial Proteins/biosynthesis,genetics DNA-Binding Proteins/biosynthesis,genetics Escherichia coli/genetics,metabolism Escherichia coli Proteins Genes, Bacterial Genes, Regulator Genotype Heat-Shock Proteins Kinetics Macromolecular Substances Mutation Protease La Serine Endopeptidases/physiology
Chemicals
Bacterial Proteins DNA-Binding Proteins Escherichia coli Proteins Heat-Shock Proteins Macromolecular Substances histone-like protein HU, bacteria ATP-Dependent Proteases Serine Endopeptidases Lon protein, E coli Protease La
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bonnefoy E
Laboratoire de Physiologie Bactérienne, Institut de Biologie Physico-Chimique, Paris, France.
Almeida A
Rouviere-Yaniv J
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26 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
Published
1989-10-00
Pages
7691-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC298136
Subset
IM
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