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
References (26)
26 references, click to expand
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