%0 Journal Article %1 Kluge2004 %A Kluge, C %A Seidel, T %A Bolte, S %A Sharma, SS %A Hanitzsch, M %A Satiat-Jeunemaitre, B %A Ross, J %A Sauer, M %A Golldack, D %A Dietz, KJ %C MIDDLESEX HOUSE, 34-42 CLEVELAND ST, LONDON W1T 4LB, ENGLAND %D 2004 %I BIOMED CENTRAL LTD %J BMC CELL BIOLOGY %K sauer %T Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex %U http://dx.doi.org/10.1186/1471-2121-5-29 %V 5 %X 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.

@article{Kluge2004, abstract = {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.}, added-at = {2011-03-01T10:57:13.000+0100}, address = {MIDDLESEX HOUSE, 34-42 CLEVELAND ST, LONDON W1T 4LB, ENGLAND}, affiliation = {Dietz, KJ (Reprint Author), Univ Bielefeld, Biochem \& Physiol Plants W5, D-33501 Bielefeld, Germany. Univ Bielefeld, Biochem \& Physiol Plants W5, D-33501 Bielefeld, Germany. CNRS, Inst Sci Vegetales, UPR 2355, F-91198 Gif Sur Yvette, France. Himachal Pradesh Univ, Dept Biosci, Shimla 171005, Himachal Prades, India. Univ Bielefeld, Appl Laser Phys \& Laser Spect D3, D-33501 Bielefeld, Germany.}, article-number = {29}, author = {Kluge, C and Seidel, T and Bolte, S and Sharma, SS and Hanitzsch, M and Satiat-Jeunemaitre, B and Ross, J and Sauer, M and Golldack, D and Dietz, KJ}, author-email = {Christoph.Kluge@isv.cnrs-gif.fr thorsten.seidel@uni-bielefeld.de Susanne.Bolte@isv.cnrs-gif.fr shantissharma@hotmail.com miriam.hanitzsch@uni-bielefeld.de bsj@isv.cnrs-gif.fr joachim.ross@physik.uni-bielefeld.de sauer@physik.uni-bielefeld.de dortje.golldack@uni-bielefeld.de karl-josef.dietz@uni-bielefeld.de}, biburl = {https://www.bibsonomy.org/bibtex/25fa857a689ee3c938c2fa545f19de6bd/reichert}, cited-references = {ABEL S, 1994, PLANT J, V5, P421. ADACHI I, 1990, J BIOL CHEM, V265, P960. BETZ M, 1991, PLANT PHYSIOL, V97, P1294. BRAIG K, 2000, STRUCT FOLD DES, V8, P567. CHANSON A, 1985, PLANT PHYSIOL, V78, P232. CHURCHILL KA, 1983, PLANT PHYSIOL, V73, P921. COOPER AA, 1996, J CELL BIOL, V133, P529. 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ZHOU ZM, 1999, J BIOL CHEM, V274, P15913.}, doc-delivery-number = {851LX}, groups = {public}, interhash = {dffe30e38a0d8c3bca14143fbef9bc0b}, intrahash = {5fa857a689ee3c938c2fa545f19de6bd}, issn = {1471-2121}, journal = {BMC CELL BIOLOGY}, journal-iso = {BMC Cell Biol.}, keywords = {sauer}, keywords-plus = {VACUOLAR H+-ATPASE; PROTON-TRANSLOCATING ATPASE; PLASMA-MEMBRANE; MESEMBRYANTHEMUM-CRYSTALLINUM; TONOPLAST POLYPEPTIDES; ENDOPLASMIC-RETICULUM; 100-KDA SUBUNIT; TERMINAL DOMAIN; CDNA CLONING; GENE ENCODES}, language = {English}, month = {AUG 13}, number-of-cited-references = {52}, publisher = {BIOMED CENTRAL LTD}, subject-category = {Cell Biology}, times-cited = {21}, timestamp = {2011-03-09T14:16:03.000+0100}, title = {Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex}, type = {Article}, unique-id = {ISI:000223687700001}, url = {http://dx.doi.org/10.1186/1471-2121-5-29}, username = {reichert}, volume = 5, year = 2004 }