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- Title
MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis.
- Authors
Kock, Holger; Gerth, Ulf; Hecker, Michael
- Abstract
The carboxyvinyl transfer from phosphoenolpyruvate to UDP- N -acetylglucosamine is the first committed step in the pathway of peptidoglycan formation. This crucial reaction for bacterial cell growth is catalysed by the MurA enzymes. Gram-negative bacteria carry one murA gene, whereas in a subgroup of Gram-positive bacteria two separate paralogues, MurAA and MurAB, exist. This study provides evidence that in the Gram-positive bacterium Bacillus subtilis , the MurAA protein is specifically degraded by the ClpCP protease. This Clp-dependent degradation is especially enhanced upon entry into stationary phase, thus ensuring an immediate growth arrest due to stalled murein biosynthesis. The MurAA protein can therefore be addressed as a target of Clp-dependent regulatory proteolysis such as the transcriptional regulators CtsR, ComK, Spx in B. subtilis , CtrA in Caulobacter crescentus or RpoS in Escherichia coli . Taking into account all other known regulatory targets of ATP-dependent proteases, MurAA of B. subtilis represents the first example of a metabolic enzyme which is a unique regulatory substrate of Clp-dependent proteolysis. Its function as a regulatory metabolic checkpoint resembles that of homoserine trans -succinylase (MetA) in E. coli which is similarly ATP-dependently degraded.
- Subjects
PYRUVATE kinase; GLYCOASPARAGINASE; PEPTIDOGLYCANS; BIOSYNTHESIS; ADENOSINE triphosphate; PROTEOLYTIC enzymes; ESCHERICHIA coli
- Publication
Molecular Microbiology, 2004, Vol 51, Issue 4, p1087
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1046/j.1365-2958.2003.03875.x