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...
Saved in:
| Main Authors: | , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
25 February 2005
|
| In: |
FEBS letters
Year: 2005, Volume: 579, Issue: 9, Pages: 1961-1967 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2005.02.042 |
| Online Access: | 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 
|
| Author Notes: | Andrea Armbrüster, Christina Hohn, Anne Hermesdorf, Karin Schumacher, Michael Börsch and Gerhard Grüber |
| Summary: | 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. |
|---|---|
| Item Description: | Gesehen am 09.08.2017 |
| Physical Description: | Online Resource |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2005.02.042 |