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J. Bacteriol. doi:10.1128/JB.01609-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Amino Acid Residues Required for Maturation, Cell Uptake, and Processing of Translation Inhibitor Microcin C

Waksman Institute, Piscataway, NJ 08854, Department of Molecular Biology and Biochemistry, Rutgers, The State University, Piscataway, NJ 08854, Institute of Protein Research, Russian Academy of Sciences, Puschino, 142292 Russia, Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, 123182 Russia

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

	Abstract

Microcin C (McC), a peptidenucleotide Trojan-horse antibiotic, targets aspartyl-tRNA synthetase. We present the results of a systematic mutational study of the seven aminoacid-long ribosomally-synthesized peptide moiety of McC. The results define amino acid positions important for McC maturation and cell uptake/processing and open way for creation of more potent McC-based inhibitors.

This article has been cited by other articles:

• Kazakov, T., Vondenhoff, G. H., Datsenko, K. A., Novikova, M., Metlitskaya, A., Wanner, B. L., Severinov, K. (2008). Escherichia coli Peptidase A, B, or N Can Process Translation Inhibitor Microcin C. J. Bacteriol. 190: 2607-2610 [Abstract] [Full Text]