The Vacuolar H+-ATPase of Clathrin-coated Vesicles Is Reversibly Inhibited by S-Nitrosoglutathione*

@article{Forgac1999TheVH,
  title={The Vacuolar H+-ATPase of Clathrin-coated Vesicles Is Reversibly Inhibited by S-Nitrosoglutathione*},
  author={Michael Forgac},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={1301 - 1305}
}
  • M. Forgac
  • Published 15 January 1999
  • Biology, Chemistry
  • The Journal of Biological Chemistry
It has been previously demonstrated that the vacuolar H+-ATPase (V-ATPase) of clathrin-coated vesicles is reversibly inhibited by disulfide bond formation between conserved cysteine residues at the catalytic site on the A subunit (Feng, Y., and Forgac, M. (1994) J. Biol. Chem. 269, 13224–13230). Proton transport and ATPase activity of the purified, reconstituted V-ATPase are now shown to be inhibited by the nitric oxide-generating reagent S-nitrosoglutathione (SNG). TheK 0.5 for inhibition by… 

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It is observed that for the purified enzyme, disulfide bond formation causes inactivation of proton transport which is reversed by dithiothreitol (DTT) and DTT also restores activity of the oxidized enzyme following treatment with N-ethylmaleimide (NEM).
Inhibition and Labeling of the Coated Vesicle V-ATPase by 2-Azido-[32P]ATP (*)
Previous studies have indicated that the 73-kDa A subunit of the coated vesicle V-ATPase possesses a nucleotide-binding site essential for activity (Arai, H., Berne, M., Terres, G., Terres, H.,
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Analysis of proteins with two-dimensional gel electrophoresis indicated that nitrate can promote the formation of disufide bonds between proteins in the vacuolar membrane, supporting the proposal by Feng and Forgac that oxidation and reduction of critical cysteine residues may regulate the activity of Vacuolar ATPases in vivo.
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