Regulation of the V-type ATPase by redox modulation

Media type: E-Article

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

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

Published: Dec 01, 2012

Language: English

DOI: 10.1042/BJ20120976

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Description: 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.

Access State: Open Access

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