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Antimicrobial Agents and Chemotherapy, November 2001, p. 3128-3131, Vol. 45, No. 11
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.11.3128-3131.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

ATP Synthase Is Necessary for Microcin H47 Antibiotic Action

Mónica Trujillo,dagger Eliana Rodríguez, and Magela Laviña*

Sección de Fisiología y Genética Bacterianas, Facultad de Ciencias, Iguá 4225, Montevideo 11.400, and División Biología Molecular, Unidad Asociada a Facultad de Ciencias, Instituto de Investigaciones Biológicas Clemente Estable, Avenida Italia 3318, Montevideo 11.600, Uruguay

Received 22 March 2001/Returned for modification 27 June 2001/Accepted 14 August 2001

Microcin H47 is a gene-encoded peptide antibiotic produced by a natural Escherichia coli strain isolated in Uruguay. In order to identify cellular components necessary for its antibiotic action, microcin H47-resistant mutants isolated in this work, as well as previously described mutants affected in membrane proteins, were analyzed. These studies indicated that (i) receptor outer membrane proteins for ferric-catechol siderophores would be involved in microcin-specific binding to the cell surface, (ii) the TonB pathway is needed for microcin H47 uptake, and (iii) the presence of the ATP synthase complex is necessary for microcin action. The possibility that this last structure contains the antibiotic target is discussed.

* Corresponding author. Mailing address: Sección de Fisiología y Genética Bacterianas, Facultad de Ciencias, Iguá 4225, Montevideo 11.400, Uruguay. Phone: (5982) 525 86 18, ext. 143. Fax: (5982) 525 86 29. E-mail: magela{at}fcien.edu.uy.

dagger Present address: Arthur and Rochelle Belfer Gene Therapy Core Facility, Weill Medicine College, Cornell University, New York, NY 10021.

Antimicrobial Agents and Chemotherapy, November 2001, p. 3128-3131, Vol. 45, No. 11
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.11.3128-3131.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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