Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding
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. Sit...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
25 February 2005
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| In: |
FEBS letters
Year: 2005, Jahrgang: 579, Heft: 9, Pages: 1961-1967 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2005.02.042 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1016/j.febslet.2005.02.042 Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2005.02.042/abstract 
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| Verfasserangaben: | Andrea Armbrüster, Christina Hohn, Anne Hermesdorf, Karin Schumacher, Michael Börsch and Gerhard Grüber |
MARC
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| 245 | 1 | 0 | |a Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding |c Andrea Armbrüster, Christina Hohn, Anne Hermesdorf, Karin Schumacher, Michael Börsch and Gerhard Grüber |
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| 520 | |a 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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