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Antimicrobial Agents and Chemotherapy, March 2001, p. 969-972, Vol. 45, No. 3
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.3.969-972.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The Structure, Function, and Origin of the Microcin H47 ATP-Binding Cassette Exporter Indicate Its Relatedness to That of Colicin V

María F. Azpiroz, Eliana Rodríguez, and Magela Laviña*

Sección de Fisiología y Genética Bacterianas, Facultad de Ciencias, Montevideo 11.400, Uruguay

Received 22 September 2000/Returned for modification 31 October 2000/Accepted 1 December 2000

Microcin H47, a gene-encoded peptide antibiotic produced by a natural Escherichia coli strain, was shown to be secreted by a three-component ATP-binding cassette exporter which was revealed to be strongly related to that of colicin V. The results of sequence and gene fusion analyses, as well as heterologous complementation assays, are presented.

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

Antimicrobial Agents and Chemotherapy, March 2001, p. 969-972, Vol. 45, No. 3
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.3.969-972.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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