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Originally published In Press as doi:10.1074/jbc.M209425200 on October 24, 2002

J. Biol. Chem., Vol. 277, Issue 52, 50867-50875, December 27, 2002
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Mutations of Bacterial RNA Polymerase Leading to Resistance to Microcin J25*

Julia Yuzenkovaabc, Monica Delgadocd, Sergei Nechaevae, Dhruti Savaliaa, Vitaly Epshteinfg, Irina Artsimovitchh, Rachel A. Mooneyi, Robert Landicki, Ricardo N. Fariasd, Raul Salomond, and Konstantin Severinovaj

From the a Department of Genetics, Waksman Institute, Piscataway, New Jersey 08854, d Instituto Superior de Investigaciones Biologicas (Consejo Nacional de Investigaciones y Technicas-Universidad Nacional de Tucuman), 4000 Tucuman, Argentina, f Public Health Research Institute, New York, New York 10016, h Department of Microbiology, Ohio State University, Columbus, Ohio 43210, and i Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706

A mutation in the conserved segment of the rpoC gene, which codes for the largest RNA polymerase (RNAP) subunit, beta ', was found to make Escherichia coli cells resistant to microcin J25 (MccJ25), a bactericidal 21-amino acid peptide active against Gram-negative bacteria (Delgado, M. A., Rintoul, M. R., Farias, R. N., and Salomon, R. A. (2001) J. Bacteriol. 183, 4543-4550). Here, we report that mutant RNAP prepared from MccJ25-resistant cells, but not the wild-type RNAP, is resistant to MccJ25 in vitro, thus establishing that RNAP is a true cellular target of MccJ25. We also report the isolation of additional rpoC mutations that lead to MccJ25 resistance in vivo and in vitro. The new mutations affect beta ' amino acids in evolutionarily conserved segments G, G', and F and are exposed into the RNAP secondary channel, a narrow opening that connects the enzyme surface with the catalytic center. We also report that previously known rpoB (RNAP beta  subunit) mutations that lead to streptolydigin resistance cause resistance to MccJ25. We hypothesize that MccJ25 inhibits transcription by binding in RNAP secondary channel and blocking substrate access to the catalytic center.

* This work was supported in part by National Institutes of Health Grants GM64307 and GM38660 (to K. S. and R. L., respectively) and by an American Society for Microbiology Arturo Sordelli fellowship (to M. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b  On leave from the Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, Russia.

c  Contributed equally to this work.

e  Present address: University of California, San Diego, La Jolla, CA.

g  Present address: Dept. of Biochemistry, NYU Medical School, New York, NY.

j  To whom correspondence should be addressed: Waksman Inst., 190 Frelinghuysen Rd., Piscataway, NJ 08854. Tel.: 732-445-6095; Fax: 732-445-5735; E-mail: severik@waksman.rutgers.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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