Affiliation:
1. Sección de Fisiología y Genética Bacterianas, Facultad de Ciencias, Montevideo, Uruguay
Abstract
ABSTRACT
It had been previously determined that the presence of F
o
F
1
ATP synthase was required for microcin H47 antibiotic action. In this work, microcin-resistant
atp
mutants were genetically analyzed. Their mutations, originated by Tn
5
insertion, in all cases were found to affect determinants for the F
o
portion of ATP synthase. To discern if microcin action required the presence of the entire complex or if the F
o
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 F
o
proton channel was absolutely required for microcin H47 action, while the F
1
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
::Tn
5
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.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Cited by
39 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献