Journal
FEBS LETTERS
Volume 579, Issue 9, Pages 1961-1967Publisher
WILEY
DOI: 10.1016/j.febslet.2005.02.042
Keywords
vacuolar-type ATPase; V1V0 ATPase; V-1; ATPase; Vma5p; VHA-C; photoaffinity labeling; fluorescence correlation spectroscopy
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The ability of subunit C of eukaryotic V-ATPases to bind ADP and ATP is demonstrated by photoaffinity labeling and fluorescence correlation spectroscopy (FCS). Quantitation of the photoaffinity and the FICS data indicate that the ATP-analogues bind more weakly to subunit C than the ADP-analogues. Site-directed mutagenesis and N-terminal sequencing of subunit C from Arabidopsis (VHA-C) and yeast (Vma5p) have been used to map the C-terminal region of subunit C as the nucleotide-binding site. Tryptophan fluorescence quenching and decreased susceptibility to tryptic digestion of subunit C after binding of different nucleotides provides evidence for structural changes in this subunit caused by nucleotide-binding. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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