Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation.

The Journal of Biological Chemistry
Elim Shao, M Forgac

Abstract

The catalytic nucleotide binding subunit (subunit A) of the vacuolar proton-translocating ATPase (or V-ATPase) is homologous to the beta-subunit of the F-ATPase but contains a 90-amino acid insert not present in the beta-subunit, termed the nonhomologous region. We previously demonstrated that mutations in this region lead to changes in coupling of proton transport and ATPase activity and to inhibition of in vivo dissociation of the V-ATPase complex, an important regulatory mechanism (Shao, E., Nishi T., Kawasaki-Nishi, S., and Forgac, M. (2003) J. Biol. Chem. 278, 12985-12991). Measurement of the ATP dependence of coupling for the wild type and mutant proteins demonstrates that the coupling differences are observed at ATP concentrations up to 1 mm. A decrease in coupling efficiency is observed at higher ATP concentrations for the wild type and mutant V-ATPases. Immunoprecipitation of an epitope-tagged nonhomologous region from cell lysates indicates that this region is able to bind to the integral V0 domain in the absence of the remainder of the A subunit, an interaction confirmed by immunoprecipitation of V0. Interaction between the nonhomologous region and V0 is reduced upon incubation of cells in the absence of glucose, sug...Continue Reading

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Citations

May 13, 2006·Journal of Bioenergetics and Biomembranes·Takao InoueMichael Forgac
May 13, 2006·Journal of Bioenergetics and Biomembranes·Patricia M Kane
Nov 28, 2007·Journal of Bioenergetics and Biomembranes·Jie QiMichael Forgac
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Jun 13, 2012·The Journal of Biological Chemistry·Yanqing XuBarry I Posner
Sep 6, 2005·The Journal of Biological Chemistry·Mali LiuPatricia M Kane
Jun 15, 2007·The Journal of Biological Chemistry·Jie Qi, Michael Forgac
May 22, 2008·The Journal of Biological Chemistry·Jie Qi, Michael Forgac
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