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Titolo:
Mitomycin resistance in Streptomyces lavendulae includes a novel drug-binding-protein-dependent export system
Autore:
Sheldon, PJ; Mao, YQ; He, M; Sherman, DH;
Indirizzi:
Univ Minnesota, Dept Microbiol, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 robiol, Minneapolis, MN 55455 USA Univ Minnesota, Biol Proc Technol Inst, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 l Inst, Minneapolis, MN 55455 USA
Titolo Testata:
JOURNAL OF BACTERIOLOGY
fascicolo: 8, volume: 181, anno: 1999,
pagine: 2507 - 2512
SICI:
0021-9193(199904)181:8<2507:MRISLI>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; TRANSPORT-SYSTEMS; TETRACYCLINE RESISTANCE; STAPHYLOCOCCUS-AUREUS; ANTISEPTIC RESISTANCE; CLONING; GENES; MECHANISM; EFFLUX; EVOLUTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Sherman, DH UnivSE,nnesota, Dept Microbiol, Box 196,1460 Mayo Mem Bldg,420Delaware St Univ Minnesota Box 196,1460 Mayo Mem Bldg,420 Delaware St SE Minneapolis MN USA 55455
Citazione:
P.J. Sheldon et al., "Mitomycin resistance in Streptomyces lavendulae includes a novel drug-binding-protein-dependent export system", J BACT, 181(8), 1999, pp. 2507-2512

Abstract

Sequence analysis of Streptomyces lavendulae NRRL 2564 chromosomal DNA adjacent to the mitomycin resistance locus rnrd (encoding a previously described mitomycin-binding protein [P. Sheldon, D. A. Johnson, P. R. August, H.-W. Liu, and D. H. Sherman, J. Bacteriol. 179:1796-1804, 1997]) revealed a putative mitomycin C (MC) transport gene (I,lct) encoding a hydrophobic polypeptide that has significant amino acid sequence similarity with several actinomycete antibiotic export proteins. Disruption of met by insertional inactivation resulted in an S. lavendulae mutant strain that was considerably more sensitive to MC. Expression of mct in Escherichia coli conferred a fivefold increase in cellular resistance to MC, led to the synthesis of a membrane-associated protein, and correlated with reduced intracellular accumulation of the drug. Coexpression of met and mrd in E. coli resulted in a 150-fold increase in resistance, as well as reduced intracellular accumulation of MC. Taken together, these data provide evidence that MRD and Met functionas components of a novel drug export system specific to the mitomycins.

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Documento generato il 03/12/20 alle ore 05:13:21