Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex
Kluge C, Seidel T, Bolte S, Sharma SS, Hanitzsch M, Satiat-Jeunemaitre B, Ross J, Sauer M, Golldack D, Dietz K-J (2004)
BMC Cell Biology 5(1): 29.
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Kluge, C;
Seidel, ThorstenUniBi;
Bolte, S;
Sharma, S. S.;
Hanitzsch, M;
Satiat-Jeunemaitre, B;
Ross, J;
Sauer, MarkusUniBi;
Golldack, DortjeUniBi;
Dietz, Karl-JosefUniBi
Einrichtung
Abstract / Bemerkung
Background: Vacuolar H+-ATPases are large protein complexes of more than 700 kDa that acidify endomembrane compartments and are part of the secretory system of eukaryotic cells. They are built from 14 different ( VHA)-subunits. The paper addresses the question of sub-cellular localisation and subunit composition of plant V-ATPase in vivo and in vitro mainly by using colocalization and fluorescence resonance energy transfer techniques ( FRET). Focus is placed on the examination and function of the 95 kDa membrane spanning subunit VHA-a. Showing similarities to the already described Vph1 and Stv1 vacuolar ATPase subunits from yeast, VHA-a revealed a bipartite structure with (i) a less conserved cytoplasmically orientated N-terminus and (ii) a membrane-spanning C-terminus with a higher extent of conservation including all amino acids shown to be essential for proton translocation in the yeast. On the basis of sequence data VHA-a appears to be an essential structural and functional element of V-ATPase, although previously a sole function in assembly has been proposed. Results: To elucidate the presence and function of VHA-a in the plant complex, three approaches were undertaken: ( i) co-immunoprecipitation with antibodies directed to epitopes in the N- and C-terminal part of VHA-a, respectively, ( ii) immunocytochemistry approach including co-localisation studies with known plant endomembrane markers, and (iii) in vivo-FRET between subunits fused to variants of green fluorescence protein (CFP, YFP) in transfected cells. Conclusions: All three sets of results show that V-ATPase contains VHA-a protein that interacts in a specific manner with other subunits. The genomes of plants encode three genes of the 95 kDa subunit ( VHA-a) of the vacuolar type H+-ATPase. Immuno-localisation of VHA-a shows that the recognized subunit is exclusively located on the endoplasmic reticulum. This result is in agreement with the hypothesis that the different isoforms of VHA-a may localize on distinct endomembrane compartments, as it was shown for its yeast counterpart Vph1.
Erscheinungsjahr
2004
Zeitschriftentitel
BMC Cell Biology
Band
5
Ausgabe
1
Seite(n)
29
ISSN
1471-2121
Page URI
https://pub.uni-bielefeld.de/record/1606782
Zitieren
Kluge C, Seidel T, Bolte S, et al. Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biology. 2004;5(1):29.
Kluge, C., Seidel, T., Bolte, S., Sharma, S. S., Hanitzsch, M., Satiat-Jeunemaitre, B., Ross, J., et al. (2004). Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biology, 5(1), 29. https://doi.org/10.1186/1471-2121-5-29
Kluge, C, Seidel, Thorsten, Bolte, S, Sharma, S. S., Hanitzsch, M, Satiat-Jeunemaitre, B, Ross, J, Sauer, Markus, Golldack, Dortje, and Dietz, Karl-Josef. 2004. “Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex”. BMC Cell Biology 5 (1): 29.
Kluge, C., Seidel, T., Bolte, S., Sharma, S. S., Hanitzsch, M., Satiat-Jeunemaitre, B., Ross, J., Sauer, M., Golldack, D., and Dietz, K. - J. (2004). Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biology 5, 29.
Kluge, C., et al., 2004. Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biology, 5(1), p 29.
C. Kluge, et al., “Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex”, BMC Cell Biology, vol. 5, 2004, pp. 29.
Kluge, C., Seidel, T., Bolte, S., Sharma, S.S., Hanitzsch, M., Satiat-Jeunemaitre, B., Ross, J., Sauer, M., Golldack, D., Dietz, K.-J.: Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biology. 5, 29 (2004).
Kluge, C, Seidel, Thorsten, Bolte, S, Sharma, S. S., Hanitzsch, M, Satiat-Jeunemaitre, B, Ross, J, Sauer, Markus, Golldack, Dortje, and Dietz, Karl-Josef. “Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex”. BMC Cell Biology 5.1 (2004): 29.
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5 Einträge gefunden, die diesen Artikel zitieren
V-type proton ATPase subunit a, vacuolar isoform (UNIPROT: P32563)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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V-type proton ATPase subunit a, Golgi isoform (UNIPROT: P37296)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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V-type proton ATPase subunit a1 (UNIPROT: Q8RWZ7)
Organism: Arabidopsis thaliana
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Organism: Arabidopsis thaliana
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V-type proton ATPase subunit a3 (UNIPROT: Q8W4S4)
Organism: Arabidopsis thaliana
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Organism: Arabidopsis thaliana
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V-type proton ATPase subunit a2 (UNIPROT: Q9SJT7)
Organism: Arabidopsis thaliana
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Organism: Arabidopsis thaliana
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Matsuoka K, Higuchi T, Maeshima M, Nakamura K., Plant Cell 9(4), 1997
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Kane PM, Parra KJ., J. Exp. Biol. 203(Pt 1), 2000
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Braig K, Menz RI, Montgomery MG, Leslie AG, Walker JE., Structure 8(6), 2000
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Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis.
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Modulation of the vacuolar H+-ATPase by adenylates as basis for the transient CO2-dependent acidification of the leaf vacuole upon illumination.
Dietz KJ, Heber U, Mimura T., Biochim. Biophys. Acta 1373(1), 1998
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Immunological characterization of two dominant tonoplast polypeptides.
Betz M, Dietz KJ., Plant Physiol. 97(4), 1991
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The vacuolar (H+)-ATPases--nature's most versatile proton pumps.
Nishi T, Forgac M., Nat. Rev. Mol. Cell Biol. 3(2), 2002
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Saturation of the endoplasmic reticulum retention machinery reveals anterograde bulk flow
Crofts AJ, Leborgne-Castel N, Hillmer S, Robinson DG, Phillipson B, Carlsson LE, Ashford DA, Denecke J., Plant Cell 11(11), 1999
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A monoclonal-antibody, JIM-84, recognizes the golgi-apparatus and plasmamembrane in plant cells
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Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants.
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Transient transformation of Arabidopsis leaf protoplasts: a versatile experimental system to study gene expression.
Abel S, Theologis A., Plant J. 5(3), 1994
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GFP-based FRET microscopy in living plant cells.
Gadella TW Jr, van der Krogt GN , Bisseling T., Trends Plant Sci. 4(7), 1999
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