메뉴 건너뛰기




Volumn 168, Issue 4, 2005, Pages 1097-1107

Characterisation of CaaX-prenyltransferases in Catharanthus roseus: Relationships with the expression of genes involved in the early stages of monoterpenoid biosynthetic pathway

Author keywords

CaaX prenyltransferases; dxr; dxs; MEP pathway; Protein farnesyltransferase; Type I protein geranylgeranyltransferase

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CHARACTERIZATION; GENES; PLANT CELL CULTURE; TISSUE;

EID: 13944258804     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2004.12.010     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • F.L. Zhang, and P.J. Casey Protein prenylation: molecular mechanisms and functional consequences Annu. Rev. Biochem. 65 1996 241 269
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 2
    • 0025819073 scopus 로고
    • Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit
    • M.C. Seabra, Y. Reiss, P.J. Casey, M.S. Brown, and J.L. Goldstein Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit Cell 65 1991 429 434
    • (1991) Cell , vol.65 , pp. 429-434
    • Seabra, M.C.1    Reiss, Y.2    Casey, P.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 3
    • 0030344706 scopus 로고    scopus 로고
    • Protein farnesyltransferase in plants: Molecular characterization and involvement in cell cycle control
    • D. Qian, D. Zhou, R. Ju, C.L. Cramer, and Z. Yang Protein farnesyltransferase in plants: molecular characterization and involvement in cell cycle control Plant Cell 8 1996 2381 2394
    • (1996) Plant Cell , vol.8 , pp. 2381-2394
    • Qian, D.1    Zhou, D.2    Ju, R.3    Cramer, C.L.4    Yang, Z.5
  • 4
    • 0029839761 scopus 로고    scopus 로고
    • A protein farnesyltransferase involved in abscissic acid signal transduction in Arabidopsis
    • S. Cutler, M. Ghassemian, D. Bonetta, S. Cooney, and P. McCourt A protein farnesyltransferase involved in abscissic acid signal transduction in Arabidopsis Science 273 1996 1239 1241
    • (1996) Science , vol.273 , pp. 1239-1241
    • Cutler, S.1    Ghassemian, M.2    Bonetta, D.3    Cooney, S.4    McCourt, P.5
  • 5
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • M. Sinensky Recent advances in the study of prenylated proteins Biochim. Biophys. Acta 1484 2000 93 106
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 6
    • 0033735850 scopus 로고    scopus 로고
    • Functional implications of protein isoprenylation in plants
    • D.N. Crowell Functional implications of protein isoprenylation in plants Prog. Lipid Res. 39 2000 393 408
    • (2000) Prog. Lipid Res. , vol.39 , pp. 393-408
    • Crowell, D.N.1
  • 7
    • 0344583793 scopus 로고    scopus 로고
    • Protein farnesylation in plants - Conserved mechanisms but different targets
    • A. Galichet, and W. Gruissem Protein farnesylation in plants - conserved mechanisms but different targets Curr. Opin. Plant Biol. 6 2003 530 535
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 530-535
    • Galichet, A.1    Gruissem, W.2
  • 9
    • 0031015862 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids in higher plant chloroplasts proceeds via a so far unexpected novel pathway
    • H.K. Lichtenthaler, J. Schwender, A. Disch, and M. Rhomer Biosynthesis of isoprenoids in higher plant chloroplasts proceeds via a so far unexpected novel pathway FEBS Lett. 400 1997 271 274
    • (1997) FEBS Lett. , vol.400 , pp. 271-274
    • Lichtenthaler, H.K.1    Schwender, J.2    Disch, A.3    Rhomer, M.4
  • 10
    • 0032423802 scopus 로고    scopus 로고
    • The iridoid glucoside secologanin is derived from the novel triose phosphate/pyruvate pathway in a Catharanthus roseus cell culture
    • A. Contin, R. van der Heijden, A.W. Lefeber, and R. Verpoorte The iridoid glucoside secologanin is derived from the novel triose phosphate/pyruvate pathway in a Catharanthus roseus cell culture FEBS Lett. 434 1998 413 416
    • (1998) FEBS Lett. , vol.434 , pp. 413-416
    • Contin, A.1    Van Der Heijden, R.2    Lefeber, A.W.3    Verpoorte, R.4
  • 11
    • 0033513375 scopus 로고    scopus 로고
    • The 1-deoxy-d-xylulose 5-phosphate pathway of isoprenoid biosynthesis in plants
    • H.K. Lichtenthaler The 1-deoxy-d-xylulose 5-phosphate pathway of isoprenoid biosynthesis in plants Annu. Rev. Plant Physiol. Plant Mol. Biol. 50 1999 47 65
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 47-65
    • Lichtenthaler, H.K.1
  • 12
    • 0033843763 scopus 로고    scopus 로고
    • 1-Deoxy-d-xylulose 5-phosphate synthase from periwinkle: CDNA identification and induced gene expression in terpenoid indole alkaloid-producing cells
    • K. Chahed, A. Oudin, N. Guivarc'h, S. Hamdi, J.-C. Chénieux, M. Rideau, and M. Clastre 1-Deoxy-d-xylulose 5-phosphate synthase from periwinkle: cDNA identification and induced gene expression in terpenoid indole alkaloid-producing cells Plant Physiol. Biochem. 38 2000 559 566
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 559-566
    • Chahed, K.1    Oudin, A.2    Guivarc'H, N.3    Hamdi, S.4    Chénieux, J.-C.5    Rideau, M.6    Clastre, M.7
  • 13
    • 0034672597 scopus 로고    scopus 로고
    • Cloning and expression of cDNAs encoding two enzymes of the MEP pathway in Catharanthus roseus
    • B. Veau, M. Courtois, A. Oudin, J.C. Chénieux, M. Rideau, and M. Clastre Cloning and expression of cDNAs encoding two enzymes of the MEP pathway in Catharanthus roseus Biochim. Biophys. Acta 1517 2000 159 163
    • (2000) Biochim. Biophys. Acta , vol.1517 , pp. 159-163
    • Veau, B.1    Courtois, M.2    Oudin, A.3    Chénieux, J.C.4    Rideau, M.5    Clastre, M.6
  • 14
    • 0037160013 scopus 로고    scopus 로고
    • Contribution of the mevalonate and methylerythritol phosphate pathways to the biosynthesis of gibberellins in Arabidopsis
    • H. Kasahara, A. Hanada, T. Kuzuyama, M. Takagi, Y. Kamiya, and S. Yamaguchi Contribution of the mevalonate and methylerythritol phosphate pathways to the biosynthesis of gibberellins in Arabidopsis J. Biol. Chem. 277 2002 45188 45194
    • (2002) J. Biol. Chem. , vol.277 , pp. 45188-45194
    • Kasahara, H.1    Hanada, A.2    Kuzuyama, T.3    Takagi, M.4    Kamiya, Y.5    Yamaguchi, S.6
  • 15
    • 1842430598 scopus 로고    scopus 로고
    • Co-expression of three MEP pathway genes and geraniol 10 hydroxylase in internal phloem parenchyma of Catharanthus roseus implicates multicellular translocation of intermediates during biosynthesis of monoterpene indole alkaloids and isoprenoid-derived primary metabolites
    • V. Burlat, A. Oudin, M. Courtois, M. Rideau, and B. St-Pierre Co-expression of three MEP pathway genes and geraniol 10 hydroxylase in internal phloem parenchyma of Catharanthus roseus implicates multicellular translocation of intermediates during biosynthesis of monoterpene indole alkaloids and isoprenoid-derived primary metabolites Plant J. 38 2004 131 141
    • (2004) Plant J. , vol.38 , pp. 131-141
    • Burlat, V.1    Oudin, A.2    Courtois, M.3    Rideau, M.4    St-Pierre, B.5
  • 16
    • 0034490132 scopus 로고    scopus 로고
    • Indole alkaloid biosynthesis in Catharanthus roseus: New enzyme activities and identification of cytochrome P450 CYP72A1 as secologanin synthase
    • S. Irmler, G. Schroder, B. St-Pierre, N.P. Crouch, M. Hotze, J. Schmidt, D. Strack, U. Matern, and J. Schroder Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450 CYP72A1 as secologanin synthase Plant J. 6 2000 797 804
    • (2000) Plant J. , vol.6 , pp. 797-804
    • Irmler, S.1    Schroder, G.2    St-Pierre, B.3    Crouch, N.P.4    Hotze, M.5    Schmidt, J.6    Strack, D.7    Matern, U.8    Schroder, J.9
  • 17
    • 0032720893 scopus 로고    scopus 로고
    • Multicellular compartmentation of Catharanthus roseus alkaloid biosynthesis predicts intercellular translocation of a pathway intermediate
    • B. St-Pierre, F.A. Vazquez-Flota, and V. DeLuca Multicellular compartmentation of Catharanthus roseus alkaloid biosynthesis predicts intercellular translocation of a pathway intermediate Plant Cell 11 1999 887 900
    • (1999) Plant Cell , vol.11 , pp. 887-900
    • St-Pierre, B.1    Vazquez-Flota, F.A.2    Deluca, V.3
  • 20
    • 0039596881 scopus 로고    scopus 로고
    • Molecular cloning and analysis of strictosidine beta-d-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus
    • A. Geerlings, M.M. Ibanez, J. Memelink, R. van Der Heijden, and R. Verpoorte Molecular cloning and analysis of strictosidine beta-d-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus J. Biol. Chem. 275 2000 3051 3056
    • (2000) J. Biol. Chem. , vol.275 , pp. 3051-3056
    • Geerlings, A.1    Ibanez, M.M.2    Memelink, J.3    Van Der Heijden, R.4    Verpoorte, R.5
  • 23
    • 0345376982 scopus 로고    scopus 로고
    • A tale of three cell types: Alkaloid biosynthesis is localized to sieve elements in opium poppy
    • D.A. Bird, V.R. Franceschi, and P.J. Facchini A tale of three cell types: alkaloid biosynthesis is localized to sieve elements in opium poppy Plant Cell 15 2003 2626 2635
    • (2003) Plant Cell , vol.15 , pp. 2626-2635
    • Bird, D.A.1    Franceschi, V.R.2    Facchini, P.J.3
  • 24
    • 0034870820 scopus 로고    scopus 로고
    • Efficient prenylation by a plant geranylgeranyltransferase-I requires a functional CaaL box motif and a proximal polybasic domain
    • D. Caldelari, H. Sternberg, M. Rodriguez-Concepcion, W. Gruissem, and S. Yalovsky Efficient prenylation by a plant geranylgeranyltransferase-I requires a functional CaaL box motif and a proximal polybasic domain Plant Physiol. 126 2001 1416 1429
    • (2001) Plant Physiol. , vol.126 , pp. 1416-1429
    • Caldelari, D.1    Sternberg, H.2    Rodriguez-Concepcion, M.3    Gruissem, W.4    Yalovsky, S.5
  • 25
    • 0026842324 scopus 로고
    • Novel repetitive sequence motifs in the α and β subunits of prenyl-protein transferases and homology of the α subunit to the MAD2 gene product of yeast
    • M.S. Boguski, A.W. Murray, and S. Powers Novel repetitive sequence motifs in the α and β subunits of prenyl-protein transferases and homology of the α subunit to the MAD2 gene product of yeast The new Biologist 4 1992 408 411
    • (1992) The New Biologist , vol.4 , pp. 408-411
    • Boguski, M.S.1    Murray, A.W.2    Powers, S.3
  • 26
    • 0344874683 scopus 로고    scopus 로고
    • Structure of mammalian protein geranylgeranyltransferase type-I
    • J.S. Taylor, T.S. Reid, K.L. Terry, P.J. Casey, and L.S. Beese Structure of mammalian protein geranylgeranyltransferase type-I EMBO J. 22 2003 5963 5974
    • (2003) EMBO J. , vol.22 , pp. 5963-5974
    • Taylor, J.S.1    Reid, T.S.2    Terry, K.L.3    Casey, P.J.4    Beese, L.S.5
  • 27
    • 0007282498 scopus 로고    scopus 로고
    • A cDNA clone encoding the beta subunit of protein farnesyltransferasefrom Nicotiana glutinosa
    • D. Zhou, Z. Yang, and C.L. Cramer A cDNA clone encoding the beta subunit of protein farnesyltransferasefrom Nicotiana glutinosa Plant Physiol. 112 1996 1399
    • (1996) Plant Physiol. , vol.112 , pp. 1399
    • Zhou, D.1    Yang, Z.2    Cramer, C.L.3
  • 29
    • 0030909826 scopus 로고    scopus 로고
    • Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
    • H.W. Park, S.R. Boduluri, J.F. Moomaw, P.J. Casey, and L.S. Beese Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution Science 275 1997 1800 1804
    • (1997) Science , vol.275 , pp. 1800-1804
    • Park, H.W.1    Boduluri, S.R.2    Moomaw, J.F.3    Casey, P.J.4    Beese, L.S.5
  • 30
    • 0032493317 scopus 로고    scopus 로고
    • Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
    • S.B. Long, P.J. Casey, and L.S. Beese Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate Biochemistry 37 1998 9612 9618
    • (1998) Biochemistry , vol.37 , pp. 9612-9618
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 32
    • 0034651550 scopus 로고    scopus 로고
    • The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 a resolution ternary complex structures
    • S.B. Long, P.J. Casey, and L.S. Beese The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures Struct. Fold Des. 8 2000 209 222
    • (2000) Struct. Fold Des. , vol.8 , pp. 209-222
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 33
    • 0034691197 scopus 로고    scopus 로고
    • Cloning of the Arabidopsis WIGGUM gene identifies a role for farnesylation in meristem development
    • E.C. Ziegelhoffer, L.J. Medrano, and E.M. Meyerowitz Cloning of the Arabidopsis WIGGUM gene identifies a role for farnesylation in meristem development Proc. Natl. Acad. Sci. U.S.A. 97 2000 7633 7638
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7633-7638
    • Ziegelhoffer, E.C.1    Medrano, L.J.2    Meyerowitz, E.M.3
  • 34
    • 0031259857 scopus 로고    scopus 로고
    • Developmental and environmental regulation of tissue- and cell-specific expression for a pea protein farnesyltransferase gene in transgenic plants
    • D. Zhou, D. Qian, C.L. Cramer, and Z. Yang Developmental and environmental regulation of tissue- and cell-specific expression for a pea protein farnesyltransferase gene in transgenic plants Plant J. 12 1997 921 930
    • (1997) Plant J. , vol.12 , pp. 921-930
    • Zhou, D.1    Qian, D.2    Cramer, C.L.3    Yang, Z.4
  • 35
    • 13944251375 scopus 로고
    • Anatomical study of the internal phloem in the stems of dicotyledons, with special reference to its histogenesis
    • Y. Fukuda Anatomical study of the internal phloem in the stems of dicotyledons, with special reference to its histogenesis J. Fac. Sci. Tokyo 9 1967 313 375
    • (1967) J. Fac. Sci. Tokyo , vol.9 , pp. 313-375
    • Fukuda, Y.1
  • 36
    • 2142765489 scopus 로고
    • Observation of the penetration of the phloem in young stems of Nerium oleander (Linn.) by stylets of the Aphid Aphis nerii (B. de F.)
    • C.E.J. Botha, S.E.-W. Mabindisa, and R.F. Evert Observation of the penetration of the phloem in young stems of Nerium oleander (Linn.) by stylets of the Aphid Aphis nerii (B. de F.) S. Afr. J. Sci. 73 1977 276 277
    • (1977) S. Afr. J. Sci. , vol.73 , pp. 276-277
    • Botha, C.E.J.1    Mabindisa, S.E.-W.2    Evert, R.F.3
  • 37
    • 0029845367 scopus 로고    scopus 로고
    • Different ratios of sucrose/raffinose-induced membrane depolarizations in the mesophyll of species with symplasmic (Catharanthus roseus, Ocimum basilicum) or apoplasmic (Impatiens walleriana, Vivia faba) minor-vein configurations
    • A.J.E. van Bel, J.H.M. Hendriks, E.J.M.C. Boon, Y.V. Gamalei, and A.P. van de Merwe Different ratios of sucrose/raffinose-induced membrane depolarizations in the mesophyll of species with symplasmic (Catharanthus roseus, Ocimum basilicum) or apoplasmic (Impatiens walleriana, Vivia faba) minor-vein configurations Planta 199 1996 185 192
    • (1996) Planta , vol.199 , pp. 185-192
    • Van Bel, A.J.E.1    Hendriks, J.H.M.2    Boon, E.J.M.C.3    Gamalei, Y.V.4    Van De Merwe, A.P.5
  • 38
    • 0032500887 scopus 로고    scopus 로고
    • Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss
    • Z.M. Pei, M. Ghassemian, C.M. Kwak, P. McCourt, and J.I. Schroeder Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss Science 282 1998 287 290
    • (1998) Science , vol.282 , pp. 287-290
    • Pei, Z.M.1    Ghassemian, M.2    Kwak, C.M.3    McCourt, P.4    Schroeder, J.I.5
  • 39
    • 0033879522 scopus 로고    scopus 로고
    • Farnesylation is involved in meristem organization in Arabidopsis
    • D. Bonetta, P. Bayliss, S. Sun, T. Sage, and P. McCourt Farnesylation is involved in meristem organization in Arabidopsis Planta 211 2000 182 190
    • (2000) Planta , vol.211 , pp. 182-190
    • Bonetta, D.1    Bayliss, P.2    Sun, S.3    Sage, T.4    McCourt, P.5
  • 40
    • 0032811420 scopus 로고    scopus 로고
    • Involvement of the octadecanoid pathway and protein phosphorylation in fungal elicitor-induced expression of terpenoid indole alkaloid biosynthetic genes in Catharanthus roseus
    • F.L. Menke, S. Parchmann, M.J. Mueller, J.W. Kijne, and J. Memelink Involvement of the octadecanoid pathway and protein phosphorylation in fungal elicitor-induced expression of terpenoid indole alkaloid biosynthetic genes in Catharanthus roseus Plant Physiol. 119 1999 1289 1296
    • (1999) Plant Physiol. , vol.119 , pp. 1289-1296
    • Menke, F.L.1    Parchmann, S.2    Mueller, M.J.3    Kijne, J.W.4    Memelink, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.