Buchumschlag

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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Bibliographische Detailangaben
Hauptverfasser: Seidel, Thorsten (VerfasserIn) , Scholl, Stefan (VerfasserIn) , Krebs, Melanie (VerfasserIn) , Rienmüller, Florian Christian (VerfasserIn) , Marten, Irene (VerfasserIn) , Hedrich, Rainer Franz (VerfasserIn) , Hanitzsch, Miriam (VerfasserIn) , Janetzki, Patricia (VerfasserIn) , Dietz, Karl-Josef (VerfasserIn) , Schumacher, Karin (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: Dec 01, 2012
In: Biochemical journal
Year: 2012, Jahrgang: 448, Heft: 2, Pages: 243-251
ISSN:1470-8728
DOI:10.1042/BJ20120976
Online-Zugang:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1042/BJ20120976
Verlag, kostenfrei, Volltext: http://www.biochemj.org/content/448/2/243
Volltext
Verfasserangaben:Thorsten Seidel, Stefan Scholl, Melanie Krebs, Florian Rienmüller, Irene Marten, Rainer Hedrich, Miriam Hanitzsch, Patricia Janetzki, Karl-Josef Dietz, Karin Schumacher
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 25.07.2017
Beschreibung:Online Resource
ISSN:1470-8728
DOI:10.1042/BJ20120976

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