Regulation of the V-type ATPase by redox modulation

Medientyp: E-Artikel

Titel: Regulation of the V-type ATPase by redox modulation

Beteiligte: Seidel, Thorsten [VerfasserIn]; Scholl, Stefan [VerfasserIn]; Krebs, Melanie [VerfasserIn]; Rienmüller, Florian Christian [VerfasserIn]; Marten, Irene [VerfasserIn]; Hedrich, Rainer Franz [VerfasserIn]; Hanitzsch, Miriam [VerfasserIn]; Janetzki, Patricia [VerfasserIn]; Dietz, Karl-Josef [VerfasserIn]; Schumacher, Karin [VerfasserIn]

Erschienen: Dec 01, 2012

Sprache: Englisch

DOI: 10.1042/BJ20120976

ISSN: 1470-8728

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Beschreibung: ATP-hydrolysis and proton pumping by the V-ATPase (vacuolar proton-translocating ATPase) are subject to redox regulation in mammals, yeast and plants. Oxidative inhibition of the V-ATPase is ascribed to disulfide-bond formation between conserved cysteine residues at the catalytic site of subunit A. Subunits containing amino acid substitutions of one of three conserved cysteine residues of VHA-A were expressed in a vha-A null mutant background in Arabidopsis. In vitro activity measurements revealed a complete absence of oxidative inhibition in the transgenic line expressing VHA-A C256S, confirming that Cys256 is necessary for redox regulation. In contrast, oxidative inhibition was unaffected in plants expressing VHA-A C279S and VHA-A C535S, indicating that disulfide bridges involving these cysteine residues are not essential for oxidative inhibition. In vivo data suggest that oxidative inhibition might not represent a general regulatory mechanism in plants.

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