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Journal of Bacteriology, April 2008, p. 2607-2610, Vol. 190, No. 7
0021-9193/08/$08.00+0 doi:10.1128/JB.01956-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Institute of Molecular Genetics, Russian Academy of Sciences, Moscow 123182, Russia,1 Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907,2 Waksman Institute, Piscataway, New Jersey 08854,3 Institute of Gene Biology, Russian Academy of Sciences, Moscow 117312, Russia4
Received 16 December 2007/ Accepted 18 January 2008
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.
Published ahead of print on 25 January 2008.
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