The Proton Channel Is the Minimal Structure of ATP Synthase Necessary and Sufficient for Microcin H47 Antibiotic Action

AUTOR(ES)

Rodríguez, Eliana

FONTE

American Society for Microbiology

RESUMO

It had been previously determined that the presence of FoF1 ATP synthase was required for microcin H47 antibiotic action. In this work, microcin-resistant atp mutants were genetically analyzed. Their mutations, originated by Tn5 insertion, in all cases were found to affect determinants for the Fo portion of ATP synthase. To discern if microcin action required the presence of the entire complex or if the Fo proton channel would suffice, recombinant plasmids carrying different segments of the atp operon were constructed and introduced into an atp deletion strain. The phenotypic analysis of the strains thus obtained clearly indicated that the presence of the Fo proton channel was absolutely required for microcin H47 action, while the F1 catalytic portion was found to be dispensable. Furthermore, when any of the three components of the proton channel was missing, total resistance to the antibiotic ensued. Complementation analysis between atp::Tn5 chromosomal mutations and recombinant atp plasmid constructions further supported the idea that the proton channel would be the minimal structure of the ATP synthase complex needed for microcin H47 antibiotic action.

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