Regulation of the V-type ATPase by redox modulation
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....
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| Main Authors: | , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
Dec 01, 2012
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| In: |
Biochemical journal
Year: 2012, Volume: 448, Issue: 2, Pages: 243-251 |
| ISSN: | 1470-8728 |
| DOI: | 10.1042/BJ20120976 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1042/BJ20120976 Verlag, kostenfrei, Volltext: http://www.biochemj.org/content/448/2/243 
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| Author Notes: | Thorsten Seidel, Stefan Scholl, Melanie Krebs, Florian Rienmüller, Irene Marten, Rainer Hedrich, Miriam Hanitzsch, Patricia Janetzki, Karl-Josef Dietz, Karin Schumacher |
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| 520 | |a 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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