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

AUTOR(ES)

Azpiroz, María F.

FONTE

American Society for Microbiology

RESUMO

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.

Documentos Relacionados

• Cloning and Characterization of the Pseudomonas fluorescens ATP-Binding Cassette Exporter, HasDEF, for the Heme Acquisition Protein HasA
• ATP Synthase Is Necessary for Microcin H47 Antibiotic Action
• ATP Synthase Is Necessary for Microcin H47 Antibiotic Action
• A Novel Bacterial ATP-Binding Cassette Transporter System That Allows Uptake of Macromolecules
• The Proton Channel Is the Minimal Structure of ATP Synthase Necessary and Sufficient for Microcin H47 Antibiotic Action