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Titolo:
Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
Autore:
St John, G; Brot, N; Ruan, J; Erdjument-Bromage, H; Tempst, P; Weissbach, H; Nathan, C;
Indirizzi:
Cornell Univ, Weill Med Coll, Grad Program Immunol, Dept Microbiol & Immunol, New York, NY 10021 USA Cornell Univ New York NY USA 10021 biol & Immunol, New York, NY 10021 USA Hosp Special Surg, New York, NY 10021 USA Hosp Special Surg New York NY USA 10021 cial Surg, New York, NY 10021 USA Sloan Kettering Inst, Prot Ctr, New York, NY 10021 USA Sloan Kettering Inst New York NY USA 10021 ot Ctr, New York, NY 10021 USA Sloan Kettering Inst, Program Mol Biol, New York, NY 10021 USA Sloan Kettering Inst New York NY USA 10021 l Biol, New York, NY 10021 USA Florida Atlantic Univ, Ctr Mol Biol & Biotechnol, Boca Raton, FL 33431 USAFlorida Atlantic Univ Boca Raton FL USA 33431 l, Boca Raton, FL 33431 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 17, volume: 98, anno: 2001,
pagine: 9901 - 9906
SICI:
0027-8424(20010814)98:17<9901:PMSRFE>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
NITRIC-OXIDE; SALMONELLA-TYPHIMURIUM; ENZYMATIC REDUCTION; MACROPHAGES; PROTEINS; GENE; PEROXYNITRITE; RESIDUES; AMINOPEPTIDASE; CYTOSTASIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Nathan, C Stanford Univ Hosp, Dept Med, Stanford, CA 94305 USA Stanford Univ Hosp Stanford CA USA 94305 Stanford, CA 94305 USA
Citazione:
G. St John et al., "Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates", P NAS US, 98(17), 2001, pp. 9901-9906

Abstract

Inducible nitric oxide synthase (iNOS) plays an important role in host defense. Macrophages expressing MOS release the reactive nitrogen intermediates (RNI) nitrite and S-nitrosoglutathlone (GSNO), which are bactericidal in vitro at a pH characteristic of the phagosome of activated macrophages. We sought to characterize the active intrabacterial forms of these RNI and their molecular targets. Peptide methionine sulfoxide reductase (MsrA; EC 1.8.4.6) catalyzes the reduction of methionine sulfoxide (Met-O) in proteins tomethionine (Met). E. coli lacking MsrA were hypersensitive to killing not only by hydrogen peroxide, but also by nitrite and GSNO. The wild-type phenotype was restored by transformation with plasmids encoding msrA from E. coli or M. tuberculosis, but not by an enzymatically inactive mutant msrA, indicating that Met oxidation was involved in the death of these cells. It seemed paradoxical that nitrite and GSNO kill bacteria by oxidizing Met residues when these RNI cannot themselves oxidize Met. However, under anaerobic conditions, neither nitrite nor GSNO was bactericidal. Nitrite and GSNO canboth give rise to NO, which may react with superoxide produced by bacteriaduring aerobic metabolism, forming peroxynitrite, a known oxidant of Met to Met-O. Thus, the findings are consistent with the hypotheses that nitriteand GSNO kill E. coli by intracellular conversion to peroxynitrite, that intracellular Met residues in proteins constitute a critical target for peroxynitrite, and that MsrA can be essential for the repair of peroxynitrite-mediated intracellular damage.

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Documento generato il 10/07/20 alle ore 16:01:21