Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements
Seidel T, Golldack D, Dietz K-J (2005)
FEBS Letters 579(20): 4374-4382.
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Einrichtung
Abstract / Bemerkung
The plant V-ATPase is a protein complex of 13 different VHA-subunits and functions as ATP driven motor that electrogenically translocates H+ into endomembrane compartments. The central rotor extends into the hexameric head that is fixed by peripheral stators to an eccentric membrane domain. The localization and orientation of VHA-subunits of the head and peripheral stalk region were investigated by in vivo fluorescence resonance energy transfer (FRET). To this end, VHA-E, VHA-G, VHA-H of the peripheral stalks as well as subunits VHA-A and VHA-B were C-terminally fused to cyan (CFP) and yellow fluorescent protein (YFP). Protoplasts transfected with FRET-pairs of CFP-donor and YFP-acceptor fluorophores fused to VHA-subunits were analysed for FRET by laser scanning microscopy. The result of the C-termini mapping allows to refine the arrangement and interaction of the subunits within the V-ATPase complex in vivo. Furthermore, expression of fused VHA-E and VHA-H stimulated acidification of protoplast vacuoles, while other constructs had no major effect on vacuolar pH tentatively indicating a regulatory role of these subunits in plants. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Stichworte
FRET;
plant;
peripheral stalk;
V-ATPase
Erscheinungsjahr
2005
Zeitschriftentitel
FEBS Letters
Band
579
Ausgabe
20
Seite(n)
4374-4382
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1602467
Zitieren
Seidel T, Golldack D, Dietz K-J. Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements. FEBS Letters. 2005;579(20):4374-4382.
Seidel, T., Golldack, D., & Dietz, K. - J. (2005). Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements. FEBS Letters, 579(20), 4374-4382. https://doi.org/10.1016/j.febslet.2005.06.077
Seidel, Thorsten, Golldack, Dortje, and Dietz, Karl-Josef. 2005. “Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements”. FEBS Letters 579 (20): 4374-4382.
Seidel, T., Golldack, D., and Dietz, K. - J. (2005). Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements. FEBS Letters 579, 4374-4382.
Seidel, T., Golldack, D., & Dietz, K.-J., 2005. Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements. FEBS Letters, 579(20), p 4374-4382.
T. Seidel, D. Golldack, and K.-J. Dietz, “Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements”, FEBS Letters, vol. 579, 2005, pp. 4374-4382.
Seidel, T., Golldack, D., Dietz, K.-J.: Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements. FEBS Letters. 579, 4374-4382 (2005).
Seidel, Thorsten, Golldack, Dortje, and Dietz, Karl-Josef. “Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements”. FEBS Letters 579.20 (2005): 4374-4382.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
INTACT
2 Einträge gefunden, die diesen Artikel zitieren
seidel-2005-1 (INTACT: EBI-7724549)
Interaction detection method: fluorescent resonance energy transfer
Interaction detection method: fluorescent resonance energy transfer
UNIPROT
7 Einträge gefunden, die diesen Artikel zitieren
V-type proton ATPase catalytic subunit A (UNIPROT: O23654)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
Vacuolar-type H+-ATPase subunit A (UNIPROT: Q0WLF6)
Organism: Arabidopsis thaliana
Download in FASTA format
Organism: Arabidopsis thaliana
Download in FASTA format
V-type proton ATPase subunit E (UNIPROT: Q40272)
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Vacuolar ATPase subunit B (UNIPROT: Q8GUB5)
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Vacuolar ATPase subunit G (UNIPROT: Q8GUB4)
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Organism: Mesembryanthemum crystallinum
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Putative vacuolar ATPase subunit H (UNIPROT: Q8GUB3)
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Putative vacuolar ATP Synthase subunit A (UNIPROT: Q9AVU8)
Organism: Mesembryanthemum crystallinum
Download in FASTA format
Organism: Mesembryanthemum crystallinum
Download in FASTA format
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Gruber G, Godovac-Zimmermann J, Link TA, Coskun U, Rizzo VF, Betz C, Bailer SM., Biochem. Biophys. Res. Commun. 298(3), 2002
PMID: 12413952
Gruber G, Godovac-Zimmermann J, Link TA, Coskun U, Rizzo VF, Betz C, Bailer SM., Biochem. Biophys. Res. Commun. 298(3), 2002
PMID: 12413952
Biochemical support for the V-ATPase rotary mechanism: antibody against HA-tagged Vma7p or Vma16p but not Vma10p inhibits activity.
Aviezer-Hagai K, Padler-Karavani V, Nelson N., J. Exp. Biol. 206(Pt 18), 2003
PMID: 12909704
Aviezer-Hagai K, Padler-Karavani V, Nelson N., J. Exp. Biol. 206(Pt 18), 2003
PMID: 12909704
Structure and assembly of the yeast V-ATPase.
Graham LA, Flannery AR, Stevens TH., J. Bioenerg. Biomembr. 35(4), 2003
PMID: 14635776
Graham LA, Flannery AR, Stevens TH., J. Bioenerg. Biomembr. 35(4), 2003
PMID: 14635776
V1-situated stalk subunits of the yeast vacuolar proton-translocating ATPase.
Tomashek JJ, Graham LA, Hutchins MU, Stevens TH, Klionsky DJ., J. Biol. Chem. 272(42), 1997
PMID: 9334266
Tomashek JJ, Graham LA, Hutchins MU, Stevens TH, Klionsky DJ., J. Biol. Chem. 272(42), 1997
PMID: 9334266
A journey from mammals to yeast with vacuolar H+-ATPase (V-ATPase).
Nelson N., J. Bioenerg. Biomembr. 35(4), 2003
PMID: 14635774
Nelson N., J. Bioenerg. Biomembr. 35(4), 2003
PMID: 14635774
Three-dimensional structure and subunit topology of the V(1) ATPase from Manduca sexta midgut.
Gruber G, Radermacher M, Ruiz T, Godovac-Zimmermann J, Canas B, Kleine-Kohlbrecher D, Huss M, Harvey WR, Wieczorek H., Biochemistry 39(29), 2000
PMID: 10913268
Gruber G, Radermacher M, Ruiz T, Godovac-Zimmermann J, Canas B, Kleine-Kohlbrecher D, Huss M, Harvey WR, Wieczorek H., Biochemistry 39(29), 2000
PMID: 10913268
The amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function.
Lu M, Vergara S, Zhang L, Holliday LS, Aris J, Gluck SL., J. Biol. Chem. 277(41), 2002
PMID: 12163484
Lu M, Vergara S, Zhang L, Holliday LS, Aris J, Gluck SL., J. Biol. Chem. 277(41), 2002
PMID: 12163484
Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A resolution.
Itoh T, Akao S, Hashimoto W, Mikami B, Murata K., J. Biol. Chem. 279(30), 2004
PMID: 15148314
Itoh T, Akao S, Hashimoto W, Mikami B, Murata K., J. Biol. Chem. 279(30), 2004
PMID: 15148314
Characterization of the functional coupling of bovine brain vacuolar-type H(+)-translocating ATPase. Effect of divalent cations, phospholipids, and subunit H (SFD).
Crider BP, Xie XS., J. Biol. Chem. 278(45), 2003
PMID: 12949075
Crider BP, Xie XS., J. Biol. Chem. 278(45), 2003
PMID: 12949075
The RAVE complex is essential for stable assembly of the yeast V-ATPase.
Smardon AM, Tarsio M, Kane PM., J. Biol. Chem. 277(16), 2002
PMID: 11844802
Smardon AM, Tarsio M, Kane PM., J. Biol. Chem. 277(16), 2002
PMID: 11844802
The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes.
Parra KJ, Keenan KL, Kane PM., J. Biol. Chem. 275(28), 2000
PMID: 10781598
Parra KJ, Keenan KL, Kane PM., J. Biol. Chem. 275(28), 2000
PMID: 10781598
Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser.
Karpova TS, Baumann CT, He L, Wu X, Grammer A, Lipsky P, Hager GL, McNally JG., J Microsc 209(Pt 1), 2003
PMID: 12535185
Karpova TS, Baumann CT, He L, Wu X, Grammer A, Lipsky P, Hager GL, McNally JG., J Microsc 209(Pt 1), 2003
PMID: 12535185
The molecular structure of green fluorescent protein.
Yang F, Moss LG, Phillips GN Jr., Nat. Biotechnol. 14(10), 1996
PMID: 9631087
Yang F, Moss LG, Phillips GN Jr., Nat. Biotechnol. 14(10), 1996
PMID: 9631087
New insight into the structure and regulation of the plant vacuolar H+-ATPase.
Kluge C, Lahr J, Hanitzsch M, Bolte S, Golldack D, Dietz KJ., J. Bioenerg. Biomembr. 35(4), 2003
PMID: 14635783
Kluge C, Lahr J, Hanitzsch M, Bolte S, Golldack D, Dietz KJ., J. Bioenerg. Biomembr. 35(4), 2003
PMID: 14635783
Three-dimensional structure of the vacuolar ATPase. Localization of subunit H by difference imaging and chemical cross-linking.
Wilkens S, Inoue T, Forgac M., J. Biol. Chem. 279(40), 2004
PMID: 15269204
Wilkens S, Inoue T, Forgac M., J. Biol. Chem. 279(40), 2004
PMID: 15269204
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