PMID:18223070
| Citation |
Kazakov, T, Vondenhoff, GH, Datsenko, KA, Novikova, M, Metlitskaya, A, Wanner, BL and Severinov, K (2008) Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C. J. Bacteriol. 190:2607-10 |
|---|---|
| Abstract |
The heptapeptide-nucleotide microcin C (McC) targets aspartyl-tRNA synthetase. Upon its entry into a susceptible cell, McC is processed to release a nonhydrolyzable aspartyl-adenylate that inhibits aspartyl-tRNA synthetase, leading to the cessation of translation and cell growth. Here, we surveyed Escherichia coli cells with singly, doubly, and triply disrupted broad-specificity peptidase genes to show that any of three nonspecific oligopeptidases (PepA, PepB, or PepN) can effectively process McC. We also show that the rate-limiting step of McC processing in vitro is deformylation of the first methionine residue of McC. |
| Links |
PubMed PMC2293190 Online version:10.1128/JB.01956-07 |
| Keywords |
Adenosine Monophosphate/analogs & derivatives; Adenosine Monophosphate/metabolism; Adenosine Monophosphate/pharmacology; Aminopeptidases/genetics; Aminopeptidases/metabolism; Aspartate-tRNA Ligase/antagonists & inhibitors; Aspartate-tRNA Ligase/metabolism; Aspartic Acid/analogs & derivatives; Aspartic Acid/metabolism; Aspartic Acid/pharmacology; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriocins/chemistry; Bacteriocins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Mass Spectrometry; Metalloendopeptidases/genetics; Metalloendopeptidases/metabolism; Molecular Structure; Mutation; Peptide Hydrolases/genetics; Peptide Hydrolases/metabolism; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism |
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