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Titolo:
Reversible redox control of plant vacuolar H+-ATPase activity is related to disulfide bridge formation in subunit E as well as subunit A
Autore:
Tavakoli, N; Kluge, C; Golldack, D; Mimura, T; Dietz, KJ;
Indirizzi:
Univ Bielefeld, Lehrstuhl Stoffwechselphysiol & Biochem Pflanzen, D-33501 Bielefeld, Germany Univ Bielefeld Bielefeld Germany D-33501 zen, D-33501 Bielefeld, Germany Nara Womens Univ, Fac Sci, Dept Biol Sci, Nara 6308506, Japan Nara Womens Univ Nara Japan 6308506 , Dept Biol Sci, Nara 6308506, Japan
Titolo Testata:
PLANT JOURNAL
fascicolo: 1, volume: 28, anno: 2001,
pagine: 51 - 59
SICI:
0960-7412(200110)28:1<51:RRCOPV>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
HORDEUM-VULGARE-L; TONOPLAST POLYPEPTIDES; TRANSPORT; CDNA; ACIDIFICATION; (H+)-ATPASE; COLEOPTILES; GLUTATHIONE; MODULATION; INHIBITION;
Keywords:
disulfide bridge formation; redox regulation; vacuole; V-ATPase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Dietz, KJ Univ Bielefeld, Lehrstuhl Stoffwechselphysiol & Biochem Pflanzen, W5, D-33501 Bielefeld, Germany Univ Bielefeld W5 Bielefeld Germany D-33501 Bielefeld, Germany
Citazione:
N. Tavakoli et al., "Reversible redox control of plant vacuolar H+-ATPase activity is related to disulfide bridge formation in subunit E as well as subunit A", PLANT J, 28(1), 2001, pp. 51-59

Abstract

The plant vacuolar proton pump can be subjected to reversible redox regulation in vitro. The redox-ependent activity change involves disulfide bridgeformation not only in Vatp A, as reported for bovine V-ATPase, but also inthe stalk subunit Vatp E. Microsomal membranes isolated from barley leaveswere analysed for their activity of bafilomycin-sensitive ATP hydrolysis and proton pumping using quinacrine fluorescence quenching in vesicle preparations. ATP hydrolysis and proton pumping activity were inhibited by H2O2. H2O2-deactivated ATPase was reactivated by cysteine and glutathione. The glutathione concentration needed for half maximal reactivation was 1 mmol l(-1). The activity loss was accompanied by shifts in electrophoretic mobilityof Vatp A and E which were reversed upon reductive reactivation. The redox-dependent shift was also seen with recombinant Vatp E, and was absent following site-directed mutagenesis of either of the two cys residues conservedthroughout all plant Vatp E sequences. V-ATPase was also inhibited by oxidized thioredoxin. These results support the hypothesis that tuning of vacuolar ATPase activity can be mediated by redox control depending on the metabolic requirements.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 14:08:05