Reference: Armbrüster A, et al. (2005) Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding. FEBS Lett 579(9):1961-7

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Abstract


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 FCS 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.

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Journal Article | Research Support, Non-U.S. Gov't
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Armbrüster A, Hohn C, Hermesdorf A, Schumacher K, Börsch M, Grüber G
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