메뉴 건너뛰기




Volumn 515, Issue , 2012, Pages 63-82

Natural rubber biosynthesis in plants: Rubber transferase

Author keywords

Cis prenyl transferase; Rubber particles; Rubber transferase

Indexed keywords

CIS ACTING ELEMENT; ENZYME ANTIBODY; RUBBER; RUBBER TRANSFERASE; TRANS ACTING FACTOR; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84866492593     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394290-6.00004-5     Document Type: Chapter
Times cited : (27)

References (38)
  • 3
    • 0038723724 scopus 로고    scopus 로고
    • Metabolic cross talk between cytosolic and plastidial pathways of isoprenoid biosynthesis: Unidirectional transport of intermediates across the chloroplast envelope membrane
    • DOI 10.1016/S0003-9861(03)00233-9
    • J.A. Bick, and B.M. Lange Metabolic cross talk between cytosolic and plastidial pathways of isoprenoid biosynthesis: Unidirectional transport of intermediates across the chloroplast envelope membrane Archives of Biochemistry and Biophysics 415 2003 146 154 (Pubitemid 36794126)
    • (2003) Archives of Biochemistry and Biophysics , vol.415 , Issue.2 , pp. 146-154
    • Bick, J.A.1    Lange, B.M.2
  • 4
    • 0032903712 scopus 로고    scopus 로고
    • Regulation of initiation and polymer molecular weight of cis-1,4- polyisoprene synthesized in vitro by particles isolated from Parthenium argentatum (Gray)
    • DOI 10.1016/S0031-9422(98)00719-5, PII S0031942298007195
    • J. Castillon, and K. Cornish Regulation of initiation and polymer molecular weight of cis-1,4-polyisoprene synthesized in vitro by particles isolated from Parthenium argentatum (Gray) Phytochemistry 51 1 1999 43 51 (Pubitemid 29232779)
    • (1999) Phytochemistry , vol.51 , Issue.1 , pp. 43-51
    • Castillon, J.1    Cornish, K.2
  • 5
    • 0027381897 scopus 로고
    • The separate roles of plant cis and trans prenyl transferases in cis-1,4-polyisoprene biosynthesis
    • DOI 10.1111/j.1432-1033.1993.tb18374.x
    • K. Cornish The separate roles of plant cis and trans prenyl transferases in cis-1,4-polyisoprene biosynthesis European Journal of Biochemistry 218 1993 267 271 (Pubitemid 23350383)
    • (1993) European Journal of Biochemistry , vol.218 , Issue.1 , pp. 267-271
    • Cornish, K.1
  • 6
    • 0035832806 scopus 로고    scopus 로고
    • Similarities and differences in rubber biochemistry among plant species
    • DOI 10.1016/S0031-9422(01)00097-8, PII S0031942201000978
    • K. Cornish Similarities and differences in rubber biochemistry among plant species Phytochemistry 57 2001 1123 1134 (Pubitemid 32625588)
    • (2001) Phytochemistry , vol.57 , Issue.7 , pp. 1123-1134
    • Cornish, K.1
  • 7
    • 0035051051 scopus 로고    scopus 로고
    • Biochemistry of natural rubber, a vital raw material, emphasizing biosynthetic rate, molecular weight and compartmentalization, in evolutionarily divergent plant species
    • K. Cornish Biochemistry of natural rubber, a vital raw material, emphasizing biosynthetic rate, molecular weight and compartmentalization, in evolutionarily divergent plant species Natural Product Reports 18 2001 182 227
    • (2001) Natural Product Reports , vol.18 , pp. 182-227
    • Cornish, K.1
  • 8
    • 0001346415 scopus 로고
    • Rubber transferase-activity in rubber particles of guayule
    • K. Cornish, and R.A. Backhaus Rubber transferase-activity in rubber particles of guayule Phytochemistry 29 1990 3809 3813
    • (1990) Phytochemistry , vol.29 , pp. 3809-3813
    • Cornish, K.1    Backhaus, R.A.2
  • 9
    • 0030913491 scopus 로고    scopus 로고
    • Stabilisation of particle integrity and particle bound cis-prenyl transferase activity in stored, purified rubber particles
    • DOI 10.1002/(SICI)1099-1565(199705)8:3<130::AID-PCA346>3.0.CO;2-0
    • K. Cornish, and D.L. Bartlett Stabilisation of particle integrity and particle-bound cis-prenyl transferase activity in stored, purified rubber particles Phytochemical Analysis 8 1997 130 134 (Pubitemid 27219988)
    • (1997) Phytochemical Analysis , vol.8 , Issue.3 , pp. 130-134
    • Cornish, K.1    Bartlett, D.L.2
  • 10
    • 19544370518 scopus 로고    scopus 로고
    • Biochemical regulation of rubber biosynthesis in guayule (Parthenium argentatum Gray)
    • DOI 10.1016/j.indcrop.2004.04.032, PII S0926669004001372, Symposium on Guayule in Honor of Dr. Francis Nakayama Held at the Association for the Advancement of Industrial Crops (AAIC) Annual
    • K. Cornish, and D.J. Scott Biochemical regulation of rubber biosynthesis in guayule (Parthenium argentatum Gray) Industrial Crops and Products 22 2005 49 58 (Pubitemid 40728294)
    • (2005) Industrial Crops and Products , vol.22 , Issue.1 , pp. 49-58
    • Cornish, K.1    Scott, D.J.2
  • 11
    • 0029177395 scopus 로고
    • Effect of different allylic diphosphates on the initiation of new rubber molecules and on Cis-1,4-polyisoprene biosynthesis in guayule (Parthenium argentatum Gray)
    • K. Cornish, and D.J. Siler Effect of different allylic diphosphates on the initiation of new rubber molecules and on cis-1,4-polyisoprene biosynthesis in guayule (Parthenium argentatum Gray) Journal of Plant Physiology 147 1995 301 305 (Pubitemid 3026294)
    • (1995) Journal of Plant Physiology , vol.147 , Issue.3-4 , pp. 301-305
    • Cornish, K.1    Siler, D.J.2
  • 12
    • 0000721910 scopus 로고    scopus 로고
    • Characterization of cis-prenyl transferase activity localised in a buoyant fraction of rubber particles from Ficus elastica latex
    • K. Cornish, and D.J. Siler Characterization of cis-prenyl transferase activity localised in a buoyant fraction of rubber particles from Ficus elastica latex Plant Physiology and Biochemistry 34 1996 377 384 (Pubitemid 126828143)
    • (1996) Plant Physiology and Biochemistry , vol.34 , Issue.3 , pp. 377-384
    • Cornish, K.1    Siler, D.J.2
  • 13
    • 0027966498 scopus 로고
    • Immunoinhibition of rubber particle-bound cis-prenyl transferases in Ficus elastica and Parthenium argentatum
    • DOI 10.1016/S0031-9422(00)86868-5
    • K. Cornish, D.J. Siler, and O.K.K. Grosjean Immunoinhibition of rubber particle-bound cis-prenyl transferases in Ficus elastica and Parthenium argentatum Phytochemistry 35 1994 1425 1428 (Pubitemid 2067865)
    • (1994) Phytochemistry , vol.35 , Issue.6 , pp. 1425-1428
    • Cornish, K.1    Siler, D.J.2    Grosjean, O.K.K.3
  • 14
    • 0033406808 scopus 로고    scopus 로고
    • Rubber particles from four different species, examined by transmission electron microscopy and electron-paramagnetic-resonance spin labeling, are found to consist of a homogeneous rubber core enclosed by a contiguous, monolayer biomembrane
    • DOI 10.1007/s004250050657
    • K. Cornish, D.F. Wood, and J.J. Windle Rubber particles from four different species, examined by transmission electron microscopy and electron-paramagnetic-resonance spin labeling, are found to consist of a homogeneous rubber core enclosed by a contiguous, monolayer biomembrane Planta 210 1999 85 96 (Pubitemid 30000919)
    • (1999) Planta , vol.210 , Issue.1 , pp. 85-96
    • Cornish, K.1    Wood, D.F.2    Windle, J.J.3
  • 15
    • 0034698361 scopus 로고    scopus 로고
    • Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis
    • DOI 10.1016/S0014-5793(00)01798-1, PII S0014579300017981
    • N. Cunillera, M. Arró, O. Forés, D. Manzano, and A. Ferrer Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis FEBS Letters 477 2000 170 174 (Pubitemid 30450161)
    • (2000) FEBS Letters , vol.477 , Issue.3 , pp. 170-174
    • Cunillera, N.1    Arro, M.2    Fores, O.3    Manzano, D.4    Ferrer, A.5
  • 16
    • 14044257708 scopus 로고    scopus 로고
    • Regulation of rubber biosynthetic rate and molecular weight in Hevea brasiliensis by metal cofactor
    • DOI 10.1021/bm049606w
    • B.M.T. da Costa, J.D. Keasling, and K. Cornish Regulation of rubber biosynthetic rate and molecular weight in Hevea brasiliensis by metal cofactor Biomacromolecules 6 2005 279 289 (Pubitemid 40277025)
    • (2005) Biomacromolecules , vol.6 , Issue.1 , pp. 279-289
    • Da Costa, B.M.T.1    Keasling, J.D.2    Cornish, K.3
  • 17
    • 33747381360 scopus 로고    scopus 로고
    • Magnesium ion regulation of in vitro rubber biosynthesis by Parthenium argentatum Gray
    • DOI 10.1016/j.phytochem.2006.04.010, PII S0031942206002160
    • B.M.T. da Costa, J.D. Keasling, C.M. McMahan, and K. Cornish Magnesium ion regulation of in vitro rubber biosynthesis by Parthenium argentatum Gray Phytochemistry 67 2006 1621 1628 (Pubitemid 44251220)
    • (2006) Phytochemistry , vol.67 , Issue.15 , pp. 1621-1628
    • Da Costa, B.M.T.1    Keasling, J.D.2    McMahan, C.M.3    Cornish, K.4
  • 19
    • 0024962575 scopus 로고
    • Rubber elongation factor from Hevea brasiliensis. Identification, characterization and role in rubber biosynthesis
    • M.S. Dennis, and D.R. Light Rubber elongation factor from Hevea brasiliensis. Identification, characterization and role in rubber biosynthesis The Journal of Biological Chemistry 264 1989 18608 18617
    • (1989) The Journal of Biological Chemistry , vol.264 , pp. 18608-18617
    • Dennis, M.S.1    Light, D.R.2
  • 21
    • 0343167441 scopus 로고    scopus 로고
    • Identification of natural rubber and characterization of rubber biosynthetic activity in fig tree
    • H. Kang, M.Y. Kang, and K.H. Han Identification of natural rubber and characterization of rubber biosynthetic activity in fig tree Plant Physiology 123 2000 1133 1142 (Pubitemid 30466865)
    • (2000) Plant Physiology , vol.123 , Issue.3 , pp. 1133-1142
    • Kang, H.1    Kang, M.Y.2    Han, K.-H.3
  • 22
    • 0037322820 scopus 로고    scopus 로고
    • Molecular analysis of cis-prenyl chain elongating enzymes
    • DOI 10.1039/b108934j
    • Y. Kharel, and T. Koyama Molecular analysis of cis-prenyl chain elongating enzymes Natural Product Reports 20 2003 111 118 (Pubitemid 36219434)
    • (2003) Natural Product Reports , vol.20 , Issue.1 , pp. 111-118
    • Kharel, Y.1    Koyama, T.2
  • 23
    • 0024962597 scopus 로고
    • Purification of a prenyl transferase that elongates cis-polyisoprene rubber from the latex of Hevea brasiliensis
    • D.R. Light, and M.S. Dennis Purification of a prenyl transferase that elongates cis-polyisoprene rubber from the latex of Hevea brasiliensis The Journal of Biological Chemistry 264 1989 18589 18597
    • (1989) The Journal of Biological Chemistry , vol.264 , pp. 18589-18597
    • Light, D.R.1    Dennis, M.S.2
  • 24
    • 0024962580 scopus 로고
    • Rubber elongation by farnesyl pyrophosphate synthases involves a novel switch in enzyme stereospecificity
    • D.R. Light, R.A. Lazarus, and M.S. Dennis Rubber elongation by farnesyl pyrophosphate synthases involves a novel switch in enzyme stereospecificity The Journal of Biological Chemistry 264 1989 18598 18607
    • (1989) The Journal of Biological Chemistry , vol.264 , pp. 18598-18607
    • Light, D.R.1    Lazarus, R.A.2    Dennis, M.S.3
  • 26
    • 0034502667 scopus 로고    scopus 로고
    • Multiwell filtration system results in rapid, high-throughput rubber transferase microassay
    • DOI 10.1002/1099-1565(200011/12)11:6<356::AID-PCA545>3.0.CO;2-A
    • C.J.D. Mau, D.J. Scott, and K. Cornish Multiwell filtration system results in rapid, high-throughput rubber transferase microassay Phytochemical Analysis 11 2000 356 361 (Pubitemid 32036931)
    • (2000) Phytochemical Analysis , vol.11 , Issue.6 , pp. 356-361
    • Mau, C.J.D.1    Scott, D.J.2    Cornish, K.3
  • 27
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • V. Neuhoff, N. Arold, D. Taube, and W. Ehrhardt Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250 Electrophoresis 9 1988 255 262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 28
    • 0034674654 scopus 로고    scopus 로고
    • Molecular cloning, expression, and functional analysis of a cis- prenyltransferase from Arabidopsis thaliana: Implications in rubber biosynthesis
    • DOI 10.1074/jbc.M002000200
    • S.K. Oh, K.H. Han, S.B. Ryu, and H. Kang Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana The Journal of Biological Chemistry 275 2000 18482 18488 (Pubitemid 30414808)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18482-18488
    • Oh, S.K.1    Han, K.H.2    Ryu, S.B.3    Kang, H.4
  • 30
    • 84857946109 scopus 로고    scopus 로고
    • Laticifer specific cis-prenyltransferase silencing affects the rubber, triterpene and inulin content of Taraxacum brevicorniculatum
    • J. Post, N. van Deenen, J. Fricke, N. Kowalski, D. Wurbs, and H. Schaller Laticifer specific cis-prenyltransferase silencing affects the rubber, triterpene and inulin content of Taraxacum brevicorniculatum Plant Physiology 154 2012
    • (2012) Plant Physiology , vol.154
    • Post, J.1    Van Deenen, N.2    Fricke, J.3    Kowalski, N.4    Wurbs, D.5    Schaller, H.6
  • 31
    • 3543072968 scopus 로고    scopus 로고
    • Purification of biotinylated proteins on streptavidin resin: A protocol for quantitative elution
    • DOI 10.1002/pmic.200300780
    • J. Rybak, S.B. Scheurer, D. Neri, and G. Elia Purification of biotinylated proteins on streptavidin resin: a protocol for quantitative elution Proteomics 4 2004 2296 2299 (Pubitemid 39025329)
    • (2004) Proteomics , vol.4 , Issue.8 , pp. 2296-2299
    • Rybak, J.-N.1    Scheurer, S.B.2    Neri, D.3    Elia, G.4
  • 32
    • 0042322332 scopus 로고    scopus 로고
    • Activation and inhibition of rubber transferases by metal cofactors and pyrophosphate substrates
    • DOI 10.1016/S0031-9422(03)00266-8
    • D.J. Scott, B.M.T. da Costa, S.C. Espy, J.D. Keasling, and K. Cornish Activation and inhibition of rubber transferases by metal cofactors and pyrophosphate substrates Phytochemistry 64 2003 123 134 (Pubitemid 37101798)
    • (2003) Phytochemistry , vol.64 , Issue.1 , pp. 123-134
    • Scott, D.J.1    Da Costa, B.M.T.2    Espy, S.C.3    Keasling, J.D.4    Cornish, K.5
  • 33
  • 34
    • 0001035422 scopus 로고
    • A protein from Ficus elastica rubber particles is related to proteins from Hevea brasiliensis and Parthenium argentatum
    • D.J. Siler, and K. Cornish A protein from Ficus elastica rubber particles is related to proteins from Hevea brasiliensis and Parthenium argentatum Phytochemistry 32 1993 1097 1102
    • (1993) Phytochemistry , vol.32 , pp. 1097-1102
    • Siler, D.J.1    Cornish, K.2
  • 35
    • 0028121244 scopus 로고
    • Identification of Parthenium argentatum rubber particle proteins immunoprecipitated by an antibody that specifically inhibits rubber transferase activity
    • DOI 10.1016/S0031-9422(00)89786-1
    • D.J. Siler, and K. Cornish Identification of Parthenium argentatum rubber particle proteins immunoprecipitated by an antibody that specifically inhibits rubber transferase activity Phytochemistry 36 1994 623 627 (Pubitemid 2097596)
    • (1994) Phytochemistry , vol.36 , Issue.3 , pp. 623-627
    • Siler, D.J.1    Cornish, K.2
  • 36
    • 0030723286 scopus 로고    scopus 로고
    • Composition of rubber particles of Hevea brasiliensis, Parthenium argentatum, Ficus elastica, and Euphorbia lactiflua indicates unconventional surface structure
    • D.J. Siler, M. Goodrich-Tanrikulu, K. Cornish, A.E. Stafford, and T.A. McKeon Composition of rubber particles of Hevea brasiliensis, Parthenium argentatum, Ficus elastica, and Euphorbia lactiflua indicates unconventional surface structure Plant Physiology and Biochemistry 35 1997 881 889 (Pubitemid 27496366)
    • (1997) Plant Physiology and Biochemistry , vol.35 , Issue.11 , pp. 881-889
    • Slier, D.J.1    Goodrich-Tanrikulu, M.2    Cornish, K.3    Stafford, A.E.4    McKeon, T.A.5
  • 37
    • 0034045387 scopus 로고    scopus 로고
    • Microstructure of purified rubber particles
    • DOI 10.1086/314269
    • D.F. Wood, and K. Cornish Microstructure of purified rubber particles International Journal of Plant Sciences 161 2000 435 445 (Pubitemid 30416533)
    • (2000) International Journal of Plant Sciences , vol.161 , Issue.3 , pp. 435-445
    • Wood, D.F.1    Cornish, K.2
  • 38
    • 56949099159 scopus 로고    scopus 로고
    • Initiation of rubber biosynthesis: In vitro comparisons of benzophenone-modified diphosphate analogues in three rubber-producing species
    • W. Xie, C.M. McMahan, A.J. DeGraw, M.D. Distefano, K. Cornish, and M.C. Whalen Initiation of rubber biosynthesis: in vitro comparisons of benzophenone-modified diphosphate analogues in three rubber-producing species Phytochemistry 69 2008 2539 2545
    • (2008) Phytochemistry , vol.69 , pp. 2539-2545
    • Xie, W.1    McMahan, C.M.2    Degraw, A.J.3    Distefano, M.D.4    Cornish, K.5    Whalen, M.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.