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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December 2012
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Research Article|
November 07 2012
Regulation of the V-type ATPase by redox modulation
Thorsten Seidel;
Thorsten Seidel
1
*Plant Biochemistry and Physiology, Faculty of Biology-W5, Bielefeld University, 33501 Bielefeld, Germany
1Correspondence may be addressed to either of these authors (email thorsten.seidel@uni-bielefeld.de or karin.schumacher@cos.uni-heidelberg.de).
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Stefan Scholl;
Stefan Scholl
†Centre for Organismal Studies (COS), University of Heidelberg, 69120 Heidelberg, Germany
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Melanie Krebs;
Melanie Krebs
†Centre for Organismal Studies (COS), University of Heidelberg, 69120 Heidelberg, Germany
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Florian Rienmüller;
Florian Rienmüller
‡Institute for Molecular Plant Physiology and Biophysics, Biocenter, University of Würzburg, 97082 Würzburg, Germany
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Irene Marten;
Irene Marten
‡Institute for Molecular Plant Physiology and Biophysics, Biocenter, University of Würzburg, 97082 Würzburg, Germany
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Rainer Hedrich;
Rainer Hedrich
‡Institute for Molecular Plant Physiology and Biophysics, Biocenter, University of Würzburg, 97082 Würzburg, Germany
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Miriam Hanitzsch;
Miriam Hanitzsch
*Plant Biochemistry and Physiology, Faculty of Biology-W5, Bielefeld University, 33501 Bielefeld, Germany
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Patricia Janetzki;
Patricia Janetzki
*Plant Biochemistry and Physiology, Faculty of Biology-W5, Bielefeld University, 33501 Bielefeld, Germany
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Karl-Josef Dietz;
Karl-Josef Dietz
*Plant Biochemistry and Physiology, Faculty of Biology-W5, Bielefeld University, 33501 Bielefeld, Germany
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Karin Schumacher
Karin Schumacher
1
†Centre for Organismal Studies (COS), University of Heidelberg, 69120 Heidelberg, Germany
1Correspondence may be addressed to either of these authors (email thorsten.seidel@uni-bielefeld.de or karin.schumacher@cos.uni-heidelberg.de).
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Publisher: Portland Press Ltd
Received:
June 15 2012
Revision Received:
August 28 2012
Accepted:
September 04 2012
Accepted Manuscript online:
September 04 2012
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 448 (2): 243–251.
Article history
Received:
June 15 2012
Revision Received:
August 28 2012
Accepted:
September 04 2012
Accepted Manuscript online:
September 04 2012
Citation
Thorsten Seidel, Stefan Scholl, Melanie Krebs, Florian Rienmüller, Irene Marten, Rainer Hedrich, Miriam Hanitzsch, Patricia Janetzki, Karl-Josef Dietz, Karin Schumacher; Regulation of the V-type ATPase by redox modulation. Biochem J 1 December 2012; 448 (2): 243–251. doi: https://doi.org/10.1042/BJ20120976
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