메뉴 건너뛰기




Volumn 5, Issue , 2004, Pages

Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; EPITOPE; GREEN FLUORESCENT PROTEIN; PROTEIN SUBUNIT; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; COMPLEMENTARY DNA; HYBRID PROTEIN; ISOPROTEIN; MEMBRANE PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; VEGETABLE PROTEIN;

EID: 10144263345     PISSN: 14712121     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2121-5-29     Document Type: Article
Times cited : (35)

References (52)
  • 1
    • 0342743221 scopus 로고
    • Membranes markers in highly purified clathrin-coated vesicles from Cucurbita hypocotyls
    • Depta H, Holstein SEH, Robinson DG, Lutzelschwab M, Michalke W: Membranes markers in highly purified clathrin-coated vesicles from Cucurbita hypocotyls. Planta 1991, 183:434-442.
    • (1991) Planta , vol.183 , pp. 434-442
    • Depta, H.1    Holstein, S.E.H.2    Robinson, D.G.3    Lutzelschwab, M.4    Michalke, W.5
  • 2
    • 0030020125 scopus 로고    scopus 로고
    • Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons
    • Robinson DG, Haschke HP, Hinz G, Hoh B, Maeshima M, Marty F: Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons. Planta 1996, 198:95-103.
    • (1996) Planta , vol.198 , pp. 95-103
    • Robinson, D.G.1    Haschke, H.P.2    Hinz, G.3    Hoh, B.4    Maeshima, M.5    Marty, F.6
  • 3
    • 0031961428 scopus 로고    scopus 로고
    • Localization of pyrophosphatase and V-ATPase in Chlamydomonas reinhardtii
    • Robinson DG, Hoppenrath M, Oberbeck K, Luykx P, Ratajczak R: Localization of pyrophosphatase and V-ATPase in Chlamydomonas reinhardtii. Bot Act 1996, 111:108-122.
    • (1996) Bot. Act , vol.111 , pp. 108-122
    • Robinson, D.G.1    Hoppenrath, M.2    Oberbeck, K.3    Luykx, P.4    Ratajczak, R.5
  • 4
    • 0142057284 scopus 로고    scopus 로고
    • Subunit structure, function, and arrangement in the yeast and coated vesicle V-ATPases
    • Inoue T, Wilkens S, Forgac M: Subunit structure, function, and arrangement in the yeast and coated vesicle V-ATPases. J Bioenerg Biomemb 2003, 35:291-299.
    • (2003) J. Bioenerg. Biomemb. , vol.35 , pp. 291-299
    • Inoue, T.1    Wilkens, S.2    Forgac, M.3
  • 5
    • 0036549017 scopus 로고    scopus 로고
    • A simple nomenclature for a complex proton pump: VHA genes encode the vacuolar H(+)-ATPase
    • Sze H, Schumacher K, Muller ML, Padmanaban S, Taiz L: A simple nomenclature for a complex proton pump: VHA genes encode the vacuolar H(+)-ATPase. Trends Plant Sci 2002, 7:157-161.
    • (2002) Trends Plant Sci. , vol.7 , pp. 157-161
    • Sze, H.1    Schumacher, K.2    Muller, M.L.3    Padmanaban, S.4    Taiz, L.5
  • 6
    • 0034786236 scopus 로고    scopus 로고
    • Significance of the V-type ATPase for the adaptation to stressful growth conditions and its regulation on the molecular and biochemical level
    • Dietz KJ, Tavakoli N, Kluge C, Mimura T, Sharma SS, Harris GC, Chardonnens AN, Golldack D: Significance of the V-type ATPase for the adaptation to stressful growth conditions and its regulation on the molecular and biochemical level. J Exp Bot 2001, 363: 969-1980.
    • (2001) J. Exp. Bot. , vol.363 , pp. 1969-1980
    • Dietz, K.J.1    Tavakoli, N.2    Kluge, C.3    Mimura, T.4    Sharma, S.S.5    Harris, G.C.6    Chardonnens, A.N.7    Golldack, D.8
  • 8
    • 0034194296 scopus 로고    scopus 로고
    • Structure, function and regulation of the plant vacuolar H(+)-translocating ATPase
    • Ratajczak R: Structure, function and regulation of the plant vacuolar H(+)-translocating ATPase. Biochim Biophys Acta 2000, 1465:17-36.
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 17-36
    • Ratajczak, R.1
  • 9
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Initiative
    • The Arabidopsis Initiative: Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 2000, 408:796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 10
    • 0038264276 scopus 로고    scopus 로고
    • cDNA cloning of 12 subunits of the V-type ATPase from Mesembryanthemum crystallinum and their expression under stress
    • Kluge C, Lamkemeyer P, Tavakoli N, Golldack D, Kandlbinder A, Dietz KJ: cDNA cloning of 12 subunits of the V-type ATPase from Mesembryanthemum crystallinum and their expression under stress. Molecular Memb Biol 2003, 20:171-183.
    • (2003) Molecular Memb. Biol. , vol.20 , pp. 171-183
    • Kluge, C.1    Lamkemeyer, P.2    Tavakoli, N.3    Golldack, D.4    Kandlbinder, A.5    Dietz, K.J.6
  • 11
    • 0025907484 scopus 로고
    • Structure of the 116 kDa polypeptide of the clathrin-coated vesicle/synaptic vesciel proton pump
    • Perin MS, Fried VA, Stone DK, Xie XS, Sudhof TC: Structure of the 116 kDa polypeptide of the clathrin-coated vesicle/synaptic vesciel proton pump. J Biol Chem 1991, 266:3877-3881.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3877-3881
    • Perin, M.S.1    Fried, V.A.2    Stone, D.K.3    Xie, X.S.4    Sudhof, T.C.5
  • 14
    • 0032992113 scopus 로고    scopus 로고
    • A 100 kDa polypeptide associates with the V0 membrane sector but not with the active oat vacuolar H(+)- ATPase, suggesting a role in assembly
    • Li X, Sze H: A 100 kDa polypeptide associates with the V0 membrane sector but not with the active oat vacuolar H(+)- ATPase, suggesting a role in assembly. Plant J 1999, 17:19-30.
    • (1999) Plant J. , vol.17 , pp. 19-30
    • Li, X.1    Sze, H.2
  • 18
    • 0029905298 scopus 로고    scopus 로고
    • Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases
    • Cooper AA, Stevens TH: Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases. J Cell Biol 1996, 133:529-541.
    • (1996) J. Cell Biol. , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 20
    • 0035940474 scopus 로고    scopus 로고
    • Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
    • Kawasaki-Nishi S, Nishi T, Forgac M: Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation. Proc Natl Acad Sci USA 2001, 98: 2397-12402.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12397-12402
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 21
    • 0028201318 scopus 로고
    • Purification and initial characterization of a potential plant vacuolar targeting receptor
    • Kirsch T, Paris N, Butler JM, Beevers L, Rogers JC: Purification and initial characterization of a potential plant vacuolar targeting receptor. Proc Natl Acad Sci USA 1994, 91: 403-3407.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3403-3407
    • Kirsch, T.1    Paris, N.2    Butler, J.M.3    Beevers, L.4    Rogers, J.C.5
  • 22
    • 0032549629 scopus 로고    scopus 로고
    • Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast VATPase
    • Leng XH, Manolson MF, Forgac M: Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast VATPase. J Biol Chem 1998, 273:6717-6723.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6717-6723
    • Leng, X.H.1    Manolson, M.F.2    Forgac, M.3
  • 23
    • 0033591450 scopus 로고    scopus 로고
    • Transmembrane topology of the 100 kDa a subunit (Vph1p) of the yeast vacuolar proton translocating ATPase
    • Leng XH, Nishi T, Forgac M: Transmembrane topology of the 100 kDa a subunit (Vph1p) of the yeast vacuolar proton translocating ATPase. J Bio Chem 1999, 274:14655-14661.
    • (1999) J. Bio. Chem. , vol.274 , pp. 14655-14661
    • Leng, X.H.1    Nishi, T.2    Forgac, M.3
  • 24
    • 0029379715 scopus 로고
    • Subunit E of the vacuolar H+-ATPase of Hordeum vulgare L.: cDNA cloning, expression and immunological analysis
    • Dietz KJ, Rudloff S, Ageorges A, Eckerskorn C, Fischer K, Arbinger B: Subunit E of the vacuolar H+-ATPase of Hordeum vulgare L.: cDNA cloning, expression and immunological analysis. Plant J 1995, 8:521-529.
    • (1995) Plant J. , vol.8 , pp. 521-529
    • Dietz, K.J.1    Rudloff, S.2    Ageorges, A.3    Eckerskorn, C.4    Fischer, K.5    Arbinger, B.6
  • 25
    • 0030575183 scopus 로고    scopus 로고
    • +-ATPase of Mesembryanthemum crystallinum L. in the CAM state: A proteolytically processed subunit B?
    • +-ATPase of Mesembryanthemum crystallinum L. in the CAM state: A proteolytically processed subunit B? FEBS Letters 1996, 389:314-318.
    • (1996) FEBS Letters , vol.389 , pp. 314-318
    • Zhigang, A.1    Low, R.2    Rausch, T.3    Lüttge, U.4    Ratajczak, R.5
  • 26
  • 27
    • 0032711298 scopus 로고    scopus 로고
    • Tonoplast intrinsic protein isoforms as markers for vacuolar functions
    • Jauh GY, Phillips TE, Rogers JC: Tonoplast intrinsic protein isoforms as markers for vacuolar functions. Plant Cell 1999, 10:1867-1882.
    • (1999) Plant Cell , vol.10 , pp. 1867-1882
    • Jauh, G.Y.1    Phillips, T.E.2    Rogers, J.C.3
  • 28
    • 0037238461 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser
    • (Oxford)
    • Karpova TS, Baumann CT, He L, Wu X, Grammer A, Lipsky P, Hager GL, McNally JG: Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J Microscopy 2003, 209:56-70. (Oxford)
    • (2003) J. Microscopy , vol.209 , pp. 56-70
    • Karpova, T.S.1    Baumann, C.T.2    He, L.3    Wu, X.4    Grammer, A.5    Lipsky, P.6    Hager, G.L.7    McNally, J.G.8
  • 29
    • 0027978351 scopus 로고
    • Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase
    • Zhang J, Feng Y, Forgac M: Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase. J Biol Chem 1994, 269(38):23518-23523.
    • (1994) J. Biol. Chem. , vol.269 , Issue.38 , pp. 23518-23523
    • Zhang, J.1    Feng, Y.2    Forgac, M.3
  • 30
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases
    • Dröse S, Altendorf K: Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J Exp Biol 1997, 200: -8.
    • (1997) J. Exp. Biol. , vol.200 , pp. 1-8
    • Dröse, S.1    Altendorf, K.2
  • 31
    • 0034782623 scopus 로고    scopus 로고
    • +-ATPase activity is related to disulfide bridge formation not only in subunit A but also in subunit E
    • +-ATPase activity is related to disulfide bridge formation not only in subunit A but also in subunit E. Plant J 2001, 28:51-60.
    • (2001) Plant J. , vol.28 , pp. 51-60
    • Tavakoli, N.1    Kluge, C.2    Golldack, D.3    Mimura, T.4    Dietz, K.J.5
  • 32
    • 0025159440 scopus 로고
    • Proteolysis and orientation on reconstitution of the coated vesicle proton pump
    • Adachi I, Arai H, Pimental R, Forgac M: Proteolysis and orientation on reconstitution of the coated vesicle proton pump. J Biol Chem 1990, 265:960-966.
    • (1990) J. Biol. Chem. , vol.265 , pp. 960-966
    • Adachi, I.1    Arai, H.2    Pimental, R.3    Forgac, M.4
  • 33
    • 0028259120 scopus 로고
    • Vacuolar-type H+-ATPases that are associated with the ER and provacuoles of root tip cells
    • Herman EM, Lix , Su RT, Larsen P, Hsu H, Sze H: Vacuolar-type H+-ATPases that are associated with the ER and provacuoles of root tip cells. Plant Physiol 1994, 106:1313-1324.
    • (1994) Plant Physiol. , vol.106 , pp. 1313-1324
    • Herman, E.M.1    Lix, A.2    Su, R.T.3    Larsen, P.4    Hsu, H.5    Sze, H.6
  • 34
    • 0028813407 scopus 로고
    • Localization of membrane pyrophosphatase activity in Ricinus communis seedlings
    • Long AR, Williams LE, Nelson SJ, Hall JI: Localization of membrane pyrophosphatase activity in Ricinus communis seedlings. J Plant Phys 1995, 146:629-638.
    • (1995) J. Plant Phys. , vol.146 , pp. 629-638
    • Long, A.R.1    Williams, L.E.2    Nelson, S.J.3    Hall, J.I.4
  • 35
    • 0028007672 scopus 로고
    • V-Type ATPase and pyrophosphatase in endomembranes of maize roots
    • Oberbeck K, Drucker M, Robinson DG: V-Type ATPase and pyrophosphatase in endomembranes of maize roots. J Exp Bot 1994, 45:235-244.
    • (1994) J. Exp. Bot. , vol.45 , pp. 235-244
    • Oberbeck, K.1    Drucker, M.2    Robinson, D.G.3
  • 36
    • 0000606120 scopus 로고
    • Evidence for an ATP-dependent proton pump on the golgi of corn coleoptiles
    • Chanson A, Taiz L: Evidence for an ATP-dependent proton pump on the golgi of corn coleoptiles. Plant Physiol 1985, 78:232-240.
    • (1985) Plant Physiol. , vol.78 , pp. 232-240
    • Chanson, A.1    Taiz, L.2
  • 38
    • 0031021175 scopus 로고    scopus 로고
    • A vacuolar-type H+-ATPase in a nonvacuolar organelle is required for the sorting of soluble vacuolar protein precursors in tobacco cells
    • Matsuoka K, Higuchi T, Maeshima ?: A vacuolar-type H+-ATPase in a nonvacuolar organelle is required for the sorting of soluble vacuolar protein precursors in tobacco cells. Plant Cell 1997, 9:533-546.
    • (1997) Plant Cell , vol.9 , pp. 533-546
    • Matsuoka, K.1    Higuchi, T.2    Maeshima, M.3
  • 39
    • 0032946360 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane protonadenosine-triphosphatases
    • Nelson N, Harvey WR: Vacuolar and plasma membrane protonadenosine-triphosphatases. Physiol Rev 1999, 79: 61-385.
    • (1999) Physiol. Rev. , vol.79 , pp. 361-385
    • Nelson, N.1    Harvey, W.R.2
  • 40
    • 0035861664 scopus 로고    scopus 로고
    • The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis
    • Kawasaki-Nishi S, Bowers K, Nishi T, Forgac M, Stevens TH: The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J Biol Chem 2001, 276:47411-47420.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47411-47420
    • Kawasaki-Nishi, S.1    Bowers, K.2    Nishi, T.3    Forgac, M.4    Stevens, T.H.5
  • 41
    • 0033974290 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H(+)-ATPase
    • Kane PM, Parra KJ: Assembly and regulation of the yeast vacuolar H(+)-ATPase. J Exp Biol 2000, 203:81-87.
    • (2000) J. Exp. Biol. , vol.203 , pp. 81-87
    • Kane, P.M.1    Parra, K.J.2
  • 42
    • 0034659905 scopus 로고    scopus 로고
    • Structure of bovine mitochondrial F1-ATPase inhibited by MgADP and aluminium fluoride
    • Braig K, Menz RI, Montgomery MG, Leslie AGW, Walker JE: Structure of bovine mitochondrial F1-ATPase inhibited by MgADP and aluminium fluoride. Structure 2000, 8:567-573.
    • (2000) Structure , vol.8 , pp. 567-573
    • Braig, K.1    Menz, R.I.2    Montgomery, M.G.3    Leslie, A.G.W.4    Walker, J.E.5
  • 43
  • 44
    • 0037252527 scopus 로고    scopus 로고
    • Divergent light-, ascorbate- and oxidative stressdependent regulation of expression of the peroxiredoxin gene family in Arabidopsis thaliana
    • Horling F, Lamkemeyer P, König J, Finkemeier I, Baier M, Kandlbinder A, Dietz KJ: Divergent light-, ascorbate- and oxidative stressdependent regulation of expression of the peroxiredoxin gene family in Arabidopsis thaliana. Plant Physiol 2003, 131:317-325.
    • (2003) Plant Physiol. , vol.131 , pp. 317-325
    • Horling, F.1    Lamkemeyer, P.2    König, J.3    Finkemeier, I.4    Baier, M.5    Kandlbinder, A.6    Dietz, K.J.7
  • 45
    • 0032516748 scopus 로고    scopus 로고
    • 2-dependent acidification of the leaf vacuole upon illumination
    • 2-dependent acidification of the leaf vacuole upon illumination. Biochim Biophys Acta 1998, 1373:87-92.
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 87-92
    • Dietz, K.J.1    Heber, U.2    Mimura, T.3
  • 46
    • 0000443911 scopus 로고
    • Immunological characterization of 2 dominant tonoplast polypeptides
    • Betz M, Dietz KJ: Immunological characterization of 2 dominant tonoplast polypeptides. Plant Physiol 1991, 97: 294-1301.
    • (1991) Plant Physiol. , vol.97 , pp. 1294-1301
    • Betz, M.1    Dietz, K.J.2
  • 47
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases-nature's most versatile proton pumps
    • Nishi T, Forgac M: The vacuolar (H+)-ATPases-nature's most versatile proton pumps. Nat Rev Mol Cell Biol 2002, 3: 4-103.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 49
    • 0001232484 scopus 로고
    • A monoclonal-antibody, JIM-84, recognizes the golgi-apparatus and plasmamembrane in plant cells
    • Horsley D, Coleman J, Evams D, Crooks K, Peart J, Satiat-Jeunemaitre B, Haws C: A monoclonal-antibody, JIM-84, recognizes the golgi-apparatus and plasmamembrane in plant cells. J Exp Bot 1993, 44(Suppl S):223-229.
    • (1993) J. Exp. Bot. , vol.44 , Issue.SUPPL. S , pp. 223-229
    • Horsley, D.1    Coleman, J.2    Evams, D.3    Crooks, K.4    Peart, J.5    Satiat-Jeunemaitre, B.6    Haws, C.7
  • 50
    • 0032030760 scopus 로고    scopus 로고
    • Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants
    • Davis SJ, Vierstra RD: Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol Biol 1998, 36:521-528.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 521-528
    • Davis, S.J.1    Vierstra, R.D.2
  • 51
    • 0028384702 scopus 로고
    • Transient transformation of Arabidopsis leaf protoplasts: A versatile experimental system to study gene expression
    • Abel S, Theologis A: Transient transformation of Arabidopsis leaf protoplasts: a versatile experimental system to study gene expression. Plant J 1994, 5:421-427.
    • (1994) Plant J. , vol.5 , pp. 421-427
    • Abel, S.1    Theologis, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.