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.
Description
Regulation of the V-type ATPase by redox modulation - PubMed
%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
}