SprE Levels Are Growth Phase Regulated in a ς S -Dependent Manner at the Level of Translation
- 15 July 2000
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 182 (14) , 4117-20
- https://doi.org/10.1128/jb.182.14.4117-4120.2000
Abstract
SprE regulates ς S levels in response to nutrient availability by promoting ClpXP-mediated degradation. Paradoxically, we observe that SprE is similarly regulated, accumulating preferentially upon starvation. This regulation of SprE levels is ς S dependent, altering SprE synthesis at the level of translation. Thus, we demonstrate that SprE and ς S function within a regulatory feedback loop.Keywords
This publication has 13 references indexed in Scilit:
- Regulation of RpoS proteolysis in Escherichia coli : The response regulator RssB is a recognition factor that interacts with the turnover element in RpoSProceedings of the National Academy of Sciences, 1999
- Regulation of RssB‐dependent proteolysis in Escherichia coli: a role for acetyl phosphate in a response regulator‐controlled processMolecular Microbiology, 1998
- The σS level in starving Escherichia coli cells increases solely as a result of its increased stability, despite decreased synthesisMolecular Microbiology, 1997
- The response regulator SprE controls the stability of RpoS.Proceedings of the National Academy of Sciences, 1996
- The response regulator RssB controls stability of the sigma(S) subunit of RNA polymerase in Escherichia coli.1996
- Identification of a central regulator of stationary‐phase gene expression in Escherichia coliMolecular Microbiology, 1991
- Improved single and multicopy lac-based cloning vectors for protein and operon fusionsGene, 1987
- Fluorographic detection of radioactivity in polyacrylamide gols with the water-soluble fluor, sodium salicylateAnalytical Biochemistry, 1979
- Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and MuJournal of Molecular Biology, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970