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PMID: 2254289 Published · ppublish English Journal Article

Proteolysis and modulation of the activity of the cell division inhibitor SulA in Escherichia coli lon mutants.

Journal of bacteriology ·Vol. 172 ·No. 12 ·1990-12-00 ·Pages 7297-300

Canceill D, Dervyn E, Huisman O

Abstract

Intracellular accumulation of the inducible cell division inhibitor SulA is modulated by proteases that ensure its degradation, namely, the Lon protease and another ATP-dependent protease(s). Lon- cells are UV sensitive because SulA is stable. We asked whether these ATP-dependent proteases are more active when lon cells are grown at high temperature or in synthetic medium since these conditions decrease the UV sensitivity of lon cells. We found that these growth conditions have no direct effect on Lon-independent degradation of SulA. They may, instead, decrease the SulA-FtsZ interaction.

MeSH Terms
ATP-Dependent Proteases Bacterial Proteins/metabolism Cell Division Energy Metabolism Escherichia coli/genetics,metabolism Escherichia coli Proteins Heat-Shock Proteins Mutation Protease La Serine Endopeptidases/metabolism Temperature
Chemicals
Bacterial Proteins Escherichia coli Proteins Heat-Shock Proteins sulA protein, E coli ATP-Dependent Proteases Serine Endopeptidases Lon protein, E coli Protease La
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Canceill D
Département de Biotechnologie, Institut Pasteur, Paris, France.
Dervyn E
Huisman O
References (20)
20 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1990-12-00
Pages
7297-300
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC210862
Subset
IM
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