메뉴 건너뛰기




Volumn 20, Issue 2, 2003, Pages 171-183

cDNA cloning of 12 subunits of the V-type ATPase from Mesembryanthemum crystallinum and their expression under stress

Author keywords

Expression analysis; M. crystallinum; Salt stress; V ATPase; vha

Indexed keywords

ADENOSINE TRIPHOSPHATASE; COMPLEMENTARY DNA; INORGANIC PYROPHOSPHATASE; MANNITOL; PROTEIN SUBUNIT;

EID: 0038264276     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/0968768031000084154     Document Type: Article
Times cited : (43)

References (43)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J. P., Leslie, A. G., Lutter, R. and Walker, J. E., 1994, Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature, 370, 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N., 1987, Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem., 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0029988965 scopus 로고    scopus 로고
    • +-ATPase in the inducible Crassulacean acid metabolism plant Mesembryanthemum crystallinum
    • +-ATPase in the inducible Crassulacean acid metabolism plant Mesembryanthemum crystallinum. Biochim. Biophys. Acta, 1281, 134-138.
    • (1996) Biochim. Biophys. Acta , vol.1281 , pp. 134-138
    • Dietz, K.J.1    Arbinger, B.2
  • 8
    • 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, K. J., Tavakoli, N., Kluge, C., Mimura, T., Sharma, S. S., Harris, G. C., Chardonnens, A. N. and Golldack, D., 2001, 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., 52, 1969-1980.
    • (2001) J. Exp. Bot. , vol.52 , 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
  • 9
  • 10
    • 0028319319 scopus 로고
    • +-ATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A
    • +-ATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A. J. Biol. Chem., 269, 13224-13230.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13224-13230
    • Feng, Y.1    Forgac, M.2
  • 12
    • 0035036231 scopus 로고    scopus 로고
    • +-ATPase in Mesembryanthemum crystallinum
    • +-ATPase in Mesembryanthemum crystallinum. Plant Physiol., 125, 1643-1654.
    • (2001) Plant Physiol. , vol.125 , pp. 1643-1654
    • Golldack, D.1    Dietz, K.-J.2
  • 14
    • 0035745766 scopus 로고    scopus 로고
    • Structure-function relationships of A-F- and V-ATPases
    • Grüber, G., Wieczorek, H., Harvey, W. R. and Muller, V., 2001, Structure-function relationships of A-, F- and V-ATPases. J. Exp. Biol., 204, 2597-2605.
    • (2001) J. Exp. Biol. , vol.204 , pp. 2597-2605
    • Grüber, G.1    Wieczorek, H.2    Harvey, W.R.3    Muller, V.4
  • 17
    • 0028877886 scopus 로고
    • +-ATPase is not always a hexamer but also a pentamer
    • +-ATPase is not always a hexamer but also a pentamer. J. Exp. Bot., 46, 1633-1636.
    • (1995) J. Exp. Bot. , vol.46 , pp. 1633-1636
    • Kramer, D.1    Mangold, B.2    Hille, A.3
  • 20
    • 0031961872 scopus 로고    scopus 로고
    • Mutational analysis of the nucleotide binding sites of the yeast vacuolar proton-translocating ATPase
    • MacLeod, K. J., Vasilyeva, E., Baleja, J. D. and Forgac, M., 1998, Mutational analysis of the nucleotide binding sites of the yeast vacuolar proton-translocating ATPase. J. Biol. Chem., 273, 150-156.
    • (1998) J. Biol. Chem. , vol.273 , pp. 150-156
    • MacLeod, K.J.1    Vasilyeva, E.2    Baleja, J.D.3    Forgac, M.4
  • 22
    • 0024279650 scopus 로고
    • cDNA sequence and homologies of the 57 kDa nucleotide binding subunit of the vacuolar ATPase from Arabidopsis
    • Manolson, M. F., Ouellette, B. F. F., Filion, M. and Poole, R. J., 1988, cDNA sequence and homologies of the 57 kDa nucleotide binding subunit of the vacuolar ATPase from Arabidopsis. J. Biol. Chem., 263, 17987-17994.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17987-17994
    • Manolson, M.F.1    Ouellette, B.F.F.2    Filion, M.3    Poole, R.J.4
  • 24
    • 0036470112 scopus 로고    scopus 로고
    • The VTC proteins in vacuole fusion: Coupling NSF activity to V0 trans-complex formation
    • Müller, O., Bayer, M., Peters, C., Andersen, S., Mann, M. and Mayer, A., 2002, The VTC proteins in vacuole fusion: coupling NSF activity to V0 trans-complex formation. EMBO J., 21, 259-269.
    • (2002) EMBO J. , vol.21 , pp. 259-269
    • Müller, O.1    Bayer, M.2    Peters, C.3    Andersen, S.4    Mann, M.5    Mayer, A.6
  • 27
    • 0035979677 scopus 로고    scopus 로고
    • Features of V-ATPases that distinguish them from F-ATPases
    • Perzov, N., Padler-Karavani, V., Nelson, H. and Nelson, N., 2001, Features of V-ATPases that distinguish them from F-ATPases. FEBS Lett., 540, 223-228.
    • (2001) FEBS Lett. , vol.540 , pp. 223-228
    • Perzov, N.1    Padler-Karavani, V.2    Nelson, H.3    Nelson, N.4
  • 28
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters, C., Bayer, M. J., Buhler, S., Andersen, J. S., Mann, M. and Mayer, A., 2001, Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature, 409, 581-588.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Buhler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 30
    • 0028082668 scopus 로고
    • +-ATPase of Mesembryanthemum crystallinum to salt stress, C3-CAM transition and plant age
    • +-ATPase of Mesembryanthemum crystallinum to salt stress, C3-CAM transition and plant age. Plant Cell Environm., 17, 1101-1112.
    • (1994) Plant Cell Environm. , vol.17 , pp. 1101-1112
    • Ratajczak, R.1    Richter, J.2    Lüttge, U.3
  • 31
    • 0030020125 scopus 로고    scopus 로고
    • Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons
    • Robinson, D. G., Haschke, H. P., Hinz, G., Hoh, B., Maeshima, M. and Marty, F., 1996, Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons. Planta, 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
  • 32
    • 0032561256 scopus 로고    scopus 로고
    • Cloning of the V-ATPase subunit G in plant: Functional expression and sub-cellular localization
    • Rouquie, D., Tournaire-Roux, C., Szponarski, W., Rossignol, M. and Doumas, P., 1998, Cloning of the V-ATPase subunit G in plant: functional expression and sub-cellular localization. FEBS Lett., 437, 287-292.
    • (1998) FEBS Lett. , vol.437 , pp. 287-292
    • Rouquie, D.1    Tournaire-Roux, C.2    Szponarski, W.3    Rossignol, M.4    Doumas, P.5
  • 33
    • 0035912787 scopus 로고    scopus 로고
    • Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae
    • Sagermann, M., Stevens, T. H. and Matthews, B. W., 2001, Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci., USA, 98, 7134-7139.
    • (2001) Proc. Natl. Acad. Sci., USA , vol.98 , pp. 7134-7139
    • Sagermann, M.1    Stevens, T.H.2    Matthews, B.W.3
  • 34
    • 0031863307 scopus 로고    scopus 로고
    • Transient ER retention as stress response: Conformational repair of heat-damaged proteins to secretion-competent structures
    • Saris, N. and Makarov, M., 1998, Transient ER retention as stress response: Conformational repair of heat-damaged proteins to secretion-competent structures. J. Cell Sci., 111, 1575-1582.
    • (1998) J. Cell Sci. , vol.111 , pp. 1575-1582
    • Saris, N.1    Makarov, M.2
  • 38
    • 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., 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
  • 39
    • 0034649566 scopus 로고    scopus 로고
    • The Arabidopsis Genome Initiative, Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Genome Initiative, 2000, Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature, 408, 796-815.
    • (2000) Nature , vol.408 , pp. 796-815


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.