%0 Journal Article %1 seidel2012regulation %A Seidel, Thorsten %A Scholl, Stefan %A Krebs, Melanie %A Rienmüller, Florian %A Marten, Irene %A Hedrich, Rainer %A Hanitzsch, Miriam %A Janetzki, Patricia %A Dietz, Karl-Josef %A Schumacher, Karin %C England %D 2012 %J The Biochemical journal %K imported %N 2 %P 243--251 %R 10.1042/BJ20120976 %T Regulation of the V-type ATPase by redox modulation %U https://pubmed.ncbi.nlm.nih.gov/22943363 %V 448 %X 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 Cys(256) 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.

@article{seidel2012regulation, abstract = {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 Cys(256) 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.}, added-at = {2024-02-16T13:34:47.000+0100}, address = {England}, author = {Seidel, Thorsten and Scholl, Stefan and Krebs, Melanie and Rienmüller, Florian and Marten, Irene and Hedrich, Rainer and Hanitzsch, Miriam and Janetzki, Patricia and Dietz, Karl-Josef and Schumacher, Karin}, biburl = {https://www.bibsonomy.org/bibtex/29c9b72d34efa282126ede4969d931f26/imarten}, comment = {22943363[pmid]}, description = {Regulation of the V-type ATPase by redox modulation - PubMed}, doi = {10.1042/BJ20120976}, interhash = {badcbbb87187255c62bc5cf37ea984b4}, intrahash = {9c9b72d34efa282126ede4969d931f26}, issn = {14708728}, journal = {The Biochemical journal}, keywords = {imported}, month = dec, number = 2, pages = {243--251}, timestamp = {2024-02-16T13:34:47.000+0100}, title = {Regulation of the V-type ATPase by redox modulation}, url = {https://pubmed.ncbi.nlm.nih.gov/22943363}, volume = 448, year = 2012 }