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J. Bacteriol. doi:10.1128/JB.01956-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

E. coli Peptidases A, B, or N Can Process Translation Inhibitor Microcin C

From the Institute of Molecular Genetics, Russian Academy of Sciences, Moscow 123182 Russia, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, Waksman Institute, Piscataway, NJ 08854, Department of Molecular Biology and Biochemistry, Rutgers, The State University, Piscataway, NJ 08854

^* To whom correspondence should be addressed. Email: severik{at}waksman.rutgers.edu.

	Abstract

The heptapeptide-nucleotide Microcin C (McC) targets aspartyl-tRNA synthetase. Upon entry into a susceptible cell, McC is processed to release a non-hydrolyzable aspartyl-adenylate that inhibits aspartyl-tRNA synthetase leading to cessation of translation and cell growth. Here, we surveyed E. coli cells with singly, doubly, and triply disrupted broad-specificity peptidase genes to show that any of three non-specific oligopeptidases (PepA, PepB, and 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.