Influence of ATP and ADP on dissociation of the V-ATPase into its V-1 and V-O complexes

Autor(en): Huss, Markus 
Wieczorek, Helmut 
Stichwörter: ADENOSINE-TRIPHOSPHATASE; ATP/ADP ratio; Biochemistry & Molecular Biology; Biophysics; Cell Biology; endogenous nucleotide; HYDROLYSIS; INHIBITION; Manduca sexta; MECHANISM; MEMBRANE; NUCLEOTIDE-BINDING-SITES; PURIFICATION; regulation; TRANSPORT; V-ATPase; VACUOLAR H+-ATPASE; VESICLE PROTON PUMP
Erscheinungsdatum: 2007
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEBS LETTERS
Volumen: 581
Ausgabe: 29
Startseite: 5566
Seitenende: 5572
Zusammenfassung: 
Although the reversible dissociation of the V1VO holoenzyme into its V-1 and V-O complexes is a general mechanism for the regulation of V-ATPases, important aspects are still not understood. By analyzing the endogenous nucleotide content of the V1VO holoenzyme and of the V-1 complex, both purified from Manduca sexta larval midgut, we found that the V-1 complex contained 1.7 molec. of ADP, whereas only 0.3 molec. of ADP were bound to the V1VO holoenzyme. By contrast, both proteins contained only negligible amounts of ATP. Incubation of the V1VO holoenzyme with various adenine nucleotides revealed that ATP hydrolysis, leading to a state containing tightly bound ADP is necessary for its dissociation. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
ISSN: 00145793
DOI: 10.1016/j.febslet.2007.11.004

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