메뉴 건너뛰기




Volumn 176, Issue 5, 2009, Pages 602-607

Vacuolar-type inorganic pyrophosphatase located on the rubber particle in the latex is an essential enzyme in regulation of the rubber biosynthesis in Hevea brasiliensis

Author keywords

Hevea brasiliensis; Jasmonic acid; Rubber biosynthesis; Rubber particle; V PPase

Indexed keywords

ARCHAEA; BACTERIA (MICROORGANISMS); HEVEA BRASILIENSIS;

EID: 61849149943     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2009.01.009     Document Type: Article
Times cited : (25)

References (41)
  • 2
    • 33644935227 scopus 로고    scopus 로고
    • +-ATPase: molecular structure and function, physiological roles and regulation
    • +-ATPase: molecular structure and function, physiological roles and regulation. J. Exp. Biol. 209 (2006) 577-589
    • (2006) J. Exp. Biol. , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 4
    • 0036481562 scopus 로고    scopus 로고
    • +-ATPase-nature's most versatile proton pumps
    • +-ATPase-nature's most versatile proton pumps. Nature 3 (2002) 94-103
    • (2002) Nature , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 5
    • 1242294379 scopus 로고    scopus 로고
    • Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography
    • Szponarski W., Sommerer N., Boyer J.C., Rossignol M., and Gibrat R. Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography. Proteomics 4 (2004) 397-406
    • (2004) Proteomics , vol.4 , pp. 397-406
    • Szponarski, W.1    Sommerer, N.2    Boyer, J.C.3    Rossignol, M.4    Gibrat, R.5
  • 6
    • 61849147511 scopus 로고
    • Evidence of an alkaline inorganic pyrophosphatase activity in the cytosol of Hevea brasiliensis latex partial purification and some characteristics of the enzyme
    • SCUTA, Hainan, PR China
    • Jacob J.L., Prevot J.C., and Vidal A. Evidence of an alkaline inorganic pyrophosphatase activity in the cytosol of Hevea brasiliensis latex partial purification and some characteristics of the enzyme. Proceedings of the Rubber Physiology and Exploitation Meeting. SCUTA, Hainan, PR China (1986) 1-20
    • (1986) Proceedings of the Rubber Physiology and Exploitation Meeting , pp. 1-20
    • Jacob, J.L.1    Prevot, J.C.2    Vidal, A.3
  • 7
    • 84971545085 scopus 로고
    • Characterization of tonoplast pyrophosphatase from Hevea brasiliensis latex
    • Siswanto, Prevot J.C., Clement A., and Jacob J.L. Characterization of tonoplast pyrophosphatase from Hevea brasiliensis latex. Indian J. Nat. Rub. Res. 7 (1994) 1-8
    • (1994) Indian J. Nat. Rub. Res. , vol.7 , pp. 1-8
    • Siswanto1    Prevot, J.C.2    Clement, A.3    Jacob, J.L.4
  • 8
    • 0009680846 scopus 로고    scopus 로고
    • The regulation of cis-polyisoprene production (natural rubber) from Hevea brasiliensis
    • D'Auzac J., Jacob J.L., and Crestin H. The regulation of cis-polyisoprene production (natural rubber) from Hevea brasiliensis. Present Res. Plant Physiol. 1 (1997) 273-331
    • (1997) Present Res. Plant Physiol. , vol.1 , pp. 273-331
    • D'Auzac, J.1    Jacob, J.L.2    Crestin, H.3
  • 9
    • 0035832806 scopus 로고    scopus 로고
    • Similarities and differences in rubber biochemistry among plant species
    • Cornish K. Similarities and differences in rubber biochemistry among plant species. Phytochemistry 57 (2001) 1123-1134
    • (2001) Phytochemistry , vol.57 , pp. 1123-1134
    • Cornish, K.1
  • 10
    • 0000199891 scopus 로고    scopus 로고
    • Isolation, characterization and functional analysis of a novel cDNA clone encoding a small rubber particle protein from Hevea brasiliensis
    • Oh S.K., Kang H., Shin D.H., Yang J., Chow K.S., Yeang H.Y., Wagner B., Breiteneder H., and Han K.H. Isolation, characterization and functional analysis of a novel cDNA clone encoding a small rubber particle protein from Hevea brasiliensis. J. Biol. Chem. 274 (1999) 17132-17138
    • (1999) J. Biol. Chem. , vol.274 , pp. 17132-17138
    • Oh, S.K.1    Kang, H.2    Shin, D.H.3    Yang, J.4    Chow, K.S.5    Yeang, H.Y.6    Wagner, B.7    Breiteneder, H.8    Han, K.H.9
  • 11
    • 0024962575 scopus 로고
    • Rubber elongation factor from Hevea brasiliensis
    • Dennis M.S., and Light D.R. Rubber elongation factor from Hevea brasiliensis. J. Biol. Chem. 264 (1989) 18608-18617
    • (1989) J. Biol. Chem. , vol.264 , pp. 18608-18617
    • Dennis, M.S.1    Light, D.R.2
  • 12
    • 0000844212 scopus 로고
    • Rubber transferase from Hevea brasiliensis latex
    • Archer B.L., and Cockbain E.G. Rubber transferase from Hevea brasiliensis latex. Methods Enzymol. 15 (1969) 476-480
    • (1969) Methods Enzymol. , vol.15 , pp. 476-480
    • Archer, B.L.1    Cockbain, E.G.2
  • 13
    • 0000721910 scopus 로고    scopus 로고
    • Characterization of cis-prenyl transferase activity localized in a buoyant fraction of rubber particles from Ficus elastica latex
    • Cornish K., and Siler D.J. Characterization of cis-prenyl transferase activity localized in a buoyant fraction of rubber particles from Ficus elastica latex. Plant Physiol. Biochem. 34 (1996) 377-384
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 377-384
    • Cornish, K.1    Siler, D.J.2
  • 14
    • 84984614508 scopus 로고
    • The relationship between the rubber transferase activity and the rubber-producing ability of rubber tree
    • Chen S.C., Shao H.S., and Hu D.Q. The relationship between the rubber transferase activity and the rubber-producing ability of rubber tree. Chin. J. Trop. Crops 15 (1994) 1-5
    • (1994) Chin. J. Trop. Crops , vol.15 , pp. 1-5
    • Chen, S.C.1    Shao, H.S.2    Hu, D.Q.3
  • 15
    • 1142293861 scopus 로고    scopus 로고
    • A novel cDNA from Parthenium argentatum Gray enhances the rubber biosynthetic activity in vitro
    • Kim I.J., Ryu S.B., Kwak Y.S., and Kang H. A novel cDNA from Parthenium argentatum Gray enhances the rubber biosynthetic activity in vitro. J. Exp. Bot. 55 (2004) 377-385
    • (2004) J. Exp. Bot. , vol.55 , pp. 377-385
    • Kim, I.J.1    Ryu, S.B.2    Kwak, Y.S.3    Kang, H.4
  • 16
    • 0000888232 scopus 로고
    • Isoprenoid biosynthesis: the Hevea factory!
    • Kush A. Isoprenoid biosynthesis: the Hevea factory!. Plant Physiol. Biochem. 32 (1994) 761-767
    • (1994) Plant Physiol. Biochem. , vol.32 , pp. 761-767
    • Kush, A.1
  • 17
    • 0031922207 scopus 로고    scopus 로고
    • Interaction of methyl jasmonate, wounding and fungal elicitation during sesquiterpene induction in Hyoscyanus muticus in root cultures
    • Singh G., Gavrieli J., Oakey J.S., and Curtis W.R. Interaction of methyl jasmonate, wounding and fungal elicitation during sesquiterpene induction in Hyoscyanus muticus in root cultures. Plant Cell Rep. 17 (1998) 391-395
    • (1998) Plant Cell Rep. , vol.17 , pp. 391-395
    • Singh, G.1    Gavrieli, J.2    Oakey, J.S.3    Curtis, W.R.4
  • 18
    • 0034647914 scopus 로고    scopus 로고
    • ORCA3, a jasmonate-responsive transcriptional regulator of plant primary and secondary metabolism
    • van der Fits L., and Memelink J. ORCA3, a jasmonate-responsive transcriptional regulator of plant primary and secondary metabolism. Science 289 (2000) 295-297
    • (2000) Science , vol.289 , pp. 295-297
    • van der Fits, L.1    Memelink, J.2
  • 19
    • 2442548678 scopus 로고    scopus 로고
    • Jasmonate and ethylene signalling and their interaction are integral parts of the elicitor signalling pathway leading to {beta}-thujaplicin biosynthesis in Cupressus lusitanica cell cultures
    • Zhao J., Zheng S.H., Fujita K., and Sakai K. Jasmonate and ethylene signalling and their interaction are integral parts of the elicitor signalling pathway leading to {beta}-thujaplicin biosynthesis in Cupressus lusitanica cell cultures. J. Exp. Bot. 55 (2004) 1003-1012
    • (2004) J. Exp. Bot. , vol.55 , pp. 1003-1012
    • Zhao, J.1    Zheng, S.H.2    Fujita, K.3    Sakai, K.4
  • 20
    • 0035984038 scopus 로고    scopus 로고
    • Methyl jasmonate induces traumatic resin ducts, terpenoid resin biosynthesis and terpenoid accumulation in developing xylem of Norway Spruce stems
    • Martin D., Tholl D., Gershenzon J., and Bohlmann J. Methyl jasmonate induces traumatic resin ducts, terpenoid resin biosynthesis and terpenoid accumulation in developing xylem of Norway Spruce stems. Plant Physiol. 129 (2002) 1003-1018
    • (2002) Plant Physiol. , vol.129 , pp. 1003-1018
    • Martin, D.1    Tholl, D.2    Gershenzon, J.3    Bohlmann, J.4
  • 21
    • 0033978824 scopus 로고    scopus 로고
    • Laticifer differentiation in Hevea brasiliensis: induced by exogenous jasmonic acid and linolenic acid
    • Hao B.Z., and Wu J.L. Laticifer differentiation in Hevea brasiliensis: induced by exogenous jasmonic acid and linolenic acid. Ann. Bot. 85 (2000) 37-43
    • (2000) Ann. Bot. , vol.85 , pp. 37-43
    • Hao, B.Z.1    Wu, J.L.2
  • 22
    • 61849085911 scopus 로고    scopus 로고
    • Studies on enzymology of the differentiation of laticiferous cells of rubber tree stimulated by exogenous JA
    • Zeng R.Z., Bai X.Q., and Li Y. Studies on enzymology of the differentiation of laticiferous cells of rubber tree stimulated by exogenous JA. Chin. J. Trop. Crops 22 (2001) 17-23
    • (2001) Chin. J. Trop. Crops , vol.22 , pp. 17-23
    • Zeng, R.Z.1    Bai, X.Q.2    Li, Y.3
  • 23
    • 61849094912 scopus 로고    scopus 로고
    • Construction of the SSH library of latex cDNA and sequence analyses of JA-stimulated rubber tree
    • Zeng R.Z., Duan C.F., and Li Y. Construction of the SSH library of latex cDNA and sequence analyses of JA-stimulated rubber tree. Chin. J. Trop. Crops 24 (2003) 1-6
    • (2003) Chin. J. Trop. Crops , vol.24 , pp. 1-6
    • Zeng, R.Z.1    Duan, C.F.2    Li, Y.3
  • 24
    • 33947577006 scopus 로고    scopus 로고
    • An alternative strategy for the membrane proteome analysis of the green sulfur bacterium chlorobium tepidum using blue native PAGE and 2-D PAGE on purified membranes
    • Aivaliotis M., Karas M., and Tsiotis G. An alternative strategy for the membrane proteome analysis of the green sulfur bacterium chlorobium tepidum using blue native PAGE and 2-D PAGE on purified membranes. J. Proteome Res. 6 (2007) 1048-1058
    • (2007) J. Proteome Res. , vol.6 , pp. 1048-1058
    • Aivaliotis, M.1    Karas, M.2    Tsiotis, G.3
  • 26
    • 0035209342 scopus 로고    scopus 로고
    • Vacuolar H(+) pyrophosphatases: from the evolutionary backwaters into the mainstream
    • Drozdowicz Y.M., and Rea P.A. Vacuolar H(+) pyrophosphatases: from the evolutionary backwaters into the mainstream. Trends Plant Sci. 6 (2001) 206-211
    • (2001) Trends Plant Sci. , vol.6 , pp. 206-211
    • Drozdowicz, Y.M.1    Rea, P.A.2
  • 27
    • 0035831442 scopus 로고    scopus 로고
    • Mutagenic analysis of functional residues in putative substrate binding site and acidic domains of vacuolar H1-pyrophosphatase
    • Nakanishi Y., Saijo T., Wada Y., and Maeshima M. Mutagenic analysis of functional residues in putative substrate binding site and acidic domains of vacuolar H1-pyrophosphatase. J. Biol. Chem. 276 (2001) 7654-7660
    • (2001) J. Biol. Chem. , vol.276 , pp. 7654-7660
    • Nakanishi, Y.1    Saijo, T.2    Wada, Y.3    Maeshima, M.4
  • 30
    • 0031104658 scopus 로고    scopus 로고
    • Identification of a methyl jasmonate-responsive region in the promoter of a lipoxygenase 1 gene expressed in barley grain
    • Rouster J., Leah R., Mundy J., and Cameron-mills V. Identification of a methyl jasmonate-responsive region in the promoter of a lipoxygenase 1 gene expressed in barley grain. Plant J. 11 (1997) 513-523
    • (1997) Plant J. , vol.11 , pp. 513-523
    • Rouster, J.1    Leah, R.2    Mundy, J.3    Cameron-mills, V.4
  • 32
    • 0005326990 scopus 로고    scopus 로고
    • +-pyrophosphatase from submitochondria particles of etiolated mung bean seedlings
    • +-pyrophosphatase from submitochondria particles of etiolated mung bean seedlings. FEBS Lett. 468 (2000) 211-214
    • (2000) FEBS Lett. , vol.468 , pp. 211-214
    • Jiang, S.S.1    Yang, S.J.2    Kuo, S.Y.3    Pan, R.L.4
  • 33
    • 0031259804 scopus 로고    scopus 로고
    • Purification and characterization of thylakoid membrane-bound inorganic pyrophosphatase from Spinacia oleracia L.
    • Jiang S.S., Fan L.L., Yang S.J., Kuo S.Y., and Pan R.L. Purification and characterization of thylakoid membrane-bound inorganic pyrophosphatase from Spinacia oleracia L. Arch. Biochem. Biophys. 346 (1997) 105-122
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 105-122
    • Jiang, S.S.1    Fan, L.L.2    Yang, S.J.3    Kuo, S.Y.4    Pan, R.L.5
  • 35
    • 0033119547 scopus 로고    scopus 로고
    • Localization of pyrophosphatase in membranes of cauliflower inflorescence cells
    • Ratajczak R., Hinz G., and Robinson D.G. Localization of pyrophosphatase in membranes of cauliflower inflorescence cells. Planta 208 (1999) 205-211
    • (1999) Planta , vol.208 , pp. 205-211
    • Ratajczak, R.1    Hinz, G.2    Robinson, D.G.3
  • 38
    • 32044457965 scopus 로고    scopus 로고
    • +-pyrophosphatase gene, SsVP, from the halophyte Suaeda salsa and its overexpression increases salt and drought tolerance of Arabidopsis
    • +-pyrophosphatase gene, SsVP, from the halophyte Suaeda salsa and its overexpression increases salt and drought tolerance of Arabidopsis. Plant Mol. Biol. 60 (2006) 41-50
    • (2006) Plant Mol. Biol. , vol.60 , pp. 41-50
    • Guo, S.1    Yin, H.2    Zhang, X.3    Zhao, F.4    Li, P.5    Chen, F.6    Zhao, Y.7    Zhang, H.8
  • 40
    • 0031992095 scopus 로고    scopus 로고
    • +-pyrophosphatase and its developmental expression in growing hypocotyl of mung bean
    • +-pyrophosphatase and its developmental expression in growing hypocotyl of mung bean. Plant Physiol. 116 (1998) 589-597
    • (1998) Plant Physiol. , vol.116 , pp. 589-597
    • Nakanishi, Y.1    Maeshima, M.2
  • 41
    • 0033179945 scopus 로고    scopus 로고
    • +-pyrophosphatase and its expression during the development of pear fruit
    • +-pyrophosphatase and its expression during the development of pear fruit. Plant Cell Physiol. 40 (1999) 900-904
    • (1999) Plant Cell Physiol. , vol.40 , pp. 900-904
    • Suzuki, Y.1    Maeshima, M.2    Yamaki, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.