메뉴 건너뛰기




Volumn 246, Issue 2, 1997, Pages 518-529

Identification of cDNAs encoding sterol methyl-transferases involved in the second methylation step of plant sterol biosynthesis

Author keywords

24 methylene lophenol; Complementation analysis; Cycloartenol; Plant sterol methyltransferase; Yeast transformation

Indexed keywords

COMPLEMENTARY DNA; METHYLTRANSFERASE; PHYTOSTEROL;

EID: 0030908496     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00518.x     Document Type: Article
Times cited : (60)

References (47)
  • 1
    • 0002864431 scopus 로고
    • Occurrence, physiology and ecology of sterols
    • University Park Press, Baltimore
    • Nes, W. R. & McKean, M. L. (1977) Occurrence, physiology and ecology of sterols, in Biochemistry of steroids and other isoprenoids, pp. 411-533, University Park Press, Baltimore.
    • (1977) Biochemistry of Steroids and Other Isoprenoids , pp. 411-533
    • Nes, W.R.1    McKean, M.L.2
  • 4
    • 0015239948 scopus 로고
    • The mechanism of introduction of alkyl groups at C-24 of stecrols. IV - Inhibition by triparanol
    • Malhotra, H. C. & Nes, W. R. (1971) The mechanism of introduction of alkyl groups at C-24 of stecrols. IV - Inhibition by triparanol, J. Biol. Chem. 246, 4934-4937.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4934-4937
    • Malhotra, H.C.1    Nes, W.R.2
  • 5
    • 0015911544 scopus 로고
    • S-Adenosyl-L-methionine-cycloarlenol methyltransferase activity in cell-free systems from Trebouxia sp. and Scenedesmus obliquus
    • Wojciechowski, Z. A., Goad, L. J. & Goodwill, T. W. (1973) S-Adenosyl-L-methionine-cycloarlenol methyltransferase activity in cell-free systems from Trebouxia sp. and Scenedesmus obliquus, Biochem. J. 136, 405-412.
    • (1973) Biochem. J. , vol.136 , pp. 405-412
    • Wojciechowski, Z.A.1    Goad, L.J.2    Goodwill, T.W.3
  • 6
    • 0021717940 scopus 로고
    • Inhibition of S-adenosyl-L-methionine sterol-C-24-methyltransferase by analogues of a carhocationic ion high-energy intermediate. Structure activity relationships for C-25 heteroatoms (N, As, S) substituted triterpenoid derivatives
    • Rahier, A., Genot, J. C., Schuber, K. Benveniste, P. & Narula, A. S. (1984) Inhibition of S-adenosyl-L-methionine sterol-C-24-methyltransferase by analogues of a carhocationic ion high-energy intermediate. Structure activity relationships for C-25 heteroatoms (N, As, S) substituted triterpenoid derivatives, J. Biol. Chem. 259, 15215-15223.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15215-15223
    • Rahier, A.1    Genot, J.C.2    Schuber, K.3    Benveniste, P.4    Narula, A.S.5
  • 8
    • 0001612646 scopus 로고
    • A 24-methylene lophenol C-28 methyltransfcmse from suspension cultures of bramble cells
    • Fonteneau, P., Hartmann-Bouillon, M. A. & Benveniste, P. (1977) A 24-methylene lophenol C-28 methyltransfcmse from suspension cultures of bramble cells, Plant Sci. Lett. 10, 147-155.
    • (1977) Plant Sci. Lett. , vol.10 , pp. 147-155
    • Fonteneau, P.1    Hartmann-Bouillon, M.A.2    Benveniste, P.3
  • 10
    • 0005193979 scopus 로고
    • 24-sterol methyl transferase: mechanism, enzymology, inhibitors and physiological importance
    • (Patterson, G. W. & Nes, W. D., eds) Am. Oil Chem. Soc. Charpaign
    • 24-sterol methyl transferase: mechanism, enzymology, inhibitors and physiological importance, in Physiology and biochemistry of sterols (Patterson, G. W. & Nes, W. D., eds) pp. 83-117, Am. Oil Chem. Soc. Charpaign.
    • (1991) Physiology and Biochemistry of Sterols , pp. 83-117
    • Janssen, G.G.1    Kalinowska, M.2    Norton, R.A.3    Nes, W.D.4
  • 11
    • 0025835715 scopus 로고
    • Differential effects of plant sterols on water permeability and on acyl chain ordering of soybean phosphatidylcholine bilayers
    • Schuler, I., Milon, A., Nakatani, Y., Ourisson, G., Albrecht, A.-M., Benveniste, P. & Hartmann, M.-A. (1991) Differential effects of plant sterols on water permeability and on acyl chain ordering of soybean phosphatidylcholine bilayers, Proc. Natl Acad. Sci. USA 88, 6926-6930.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6926-6930
    • Schuler, I.1    Milon, A.2    Nakatani, Y.3    Ourisson, G.4    Albrecht, A.-M.5    Benveniste, P.6    Hartmann, M.-A.7
  • 13
    • 0030030157 scopus 로고    scopus 로고
    • Transformation of Saccharomyces cerevisiae with a cDNA encoding a sterol C-methyltransferase from Arabidopsis thaliana results in the synthesis of 24-ethyl sterols
    • Husselstein, T. Gachotte, D., Desprez, T., Bard, M. & Benveniste, P. (1996) Transformation of Saccharomyces cerevisiae with a cDNA encoding a sterol C-methyltransferase from Arabidopsis thaliana results in the synthesis of 24-ethyl sterols, FEBS Lett. 381, 87-92.
    • (1996) FEBS Lett. , vol.381 , pp. 87-92
    • Husselstein, T.1    Gachotte, D.2    Desprez, T.3    Bard, M.4    Benveniste, P.5
  • 14
    • 0029079397 scopus 로고
    • Identification ot cDNA clones encoding valosin-containing protein and other plant plasma membrane-associated proteins by a general immunoscreening strategy
    • Shi, J., Dixon, R. A., Gonzales, R. A., Kjellborn, P. & Bhattacharyya, M. K. (1995) Identification ot cDNA clones encoding valosin-containing protein and other plant plasma membrane-associated proteins by a general immunoscreening strategy, Proc. Natl Acad. Sci. USA 92, 4457-4461.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4457-4461
    • Shi, J.1    Dixon, R.A.2    Gonzales, R.A.3    Kjellborn, P.4    Bhattacharyya, M.K.5
  • 15
    • 0024999601 scopus 로고
    • Maximizing the expression of mammalian cytochrome P450 monooxygenase activities in yeast cells
    • Urban, P., Cullin, C. & Pompon, D. (1990) Maximizing the expression of mammalian cytochrome P450 monooxygenase activities in yeast cells, Biochimie (Paris) 72, 463-472.
    • (1990) Biochimie (Paris) , vol.72 , pp. 463-472
    • Urban, P.1    Cullin, C.2    Pompon, D.3
  • 17
    • 0026939004 scopus 로고
    • Isolation of the Ambidopsis ABI3 gene by positional cloning
    • Giraudat, J., Hause, B. M., Valon, C. & Smalle, J. (1992) Isolation of the Ambidopsis ABI3 gene by positional cloning, Plant Cell 4, 1251-1261.
    • (1992) Plant Cell , vol.4 , pp. 1251-1261
    • Giraudat, J.1    Hause, B.M.2    Valon, C.3    Smalle, J.4
  • 19
    • 0024799254 scopus 로고
    • High efficiency transformation of intact cells using single stranded nucleic acids as a carrier
    • Schiestl, R. H. & Gietz, R. D. (1989) High efficiency transformation of intact cells using single stranded nucleic acids as a carrier, Curr. Genet. 16, 339-346.
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 20
    • 0030111416 scopus 로고    scopus 로고
    • Isolation and characterization of an Arabidopsis thaliana cDNA encoding a A'-sterol-C-5-desaturase by functional complementation of a defective yeast mutant
    • Gachotte, D., Husselstein, T. Bard, M., Lacroute, F. & Benveniste, P. (1996) Isolation and characterization of an Arabidopsis thaliana cDNA encoding a A'-sterol-C-5-desaturase by functional complementation of a defective yeast mutant, Plant J. 9, 391-398.
    • (1996) Plant J. , vol.9 , pp. 391-398
    • Gachotte, D.1    Husselstein, T.2    Bard, M.3    Lacroute, F.4    Benveniste, P.5
  • 21
    • 0001666908 scopus 로고
    • Effect of AY-9944 on sterol biosynthesis in suspension cultures of bramble cells
    • Schmitt, P. & Benveniste, P. (1979) Effect of AY-9944 on sterol biosynthesis in suspension cultures of bramble cells, Phytochemistry 18, 445-450.
    • (1979) Phytochemistry , vol.18 , pp. 445-450
    • Schmitt, P.1    Benveniste, P.2
  • 22
    • 0002286114 scopus 로고
    • Mass spectral identification of phytosterols
    • (Nes, W. D. & Parish, E., eds) Academic Press Inc., San Diego
    • Rahier, A. & Benveniste, P. (1989) Mass spectral identification of phytosterols, in Analysis of sterols and other biologically significant steroids (Nes, W. D. & Parish, E., eds) pp. 223-249, Academic Press Inc., San Diego.
    • (1989) Analysis of Sterols and Other Biologically Significant Steroids , pp. 223-249
    • Rahier, A.1    Benveniste, P.2
  • 23
    • 0039095900 scopus 로고
    • The identification of 24-methylene-24,25-dihydrolanosterol and other possible ergosterol precursors in Phycomyces blakesleeanus and Agaricus campestris
    • Goulston, G., Mercer, E. I. & Goad, L. J. (1975) The identification of 24-methylene-24,25-dihydrolanosterol and other possible ergosterol precursors in Phycomyces blakesleeanus and Agaricus campestris, Phytochemistry 14, 457-462.
    • (1975) Phytochemistry , vol.14 , pp. 457-462
    • Goulston, G.1    Mercer, E.I.2    Goad, L.J.3
  • 24
    • 8244250590 scopus 로고
    • Sitosterol biosynthesis in Hordeum vulgare
    • Lenton, J. R., Goad, L. J. & Goodwill, T. W. (1975) Sitosterol biosynthesis in Hordeum vulgare, Phytochemistry 14, 1523-1528.
    • (1975) Phytochemistry , vol.14 , pp. 1523-1528
    • Lenton, J.R.1    Goad, L.J.2    Goodwill, T.W.3
  • 25
    • 0028119083 scopus 로고
    • Sterol overproduction is the biochemical basis of resistance to a triazole in calli from a tobacco mutant
    • Schaller, H., Gondet, L., Maillot-Vernier, P. & Benveniste, P. (1994) Sterol overproduction is the biochemical basis of resistance to a triazole in calli from a tobacco mutant, Planta (Heidelb.) 194, 295-305.
    • (1994) Planta (Heidelb.) , vol.194 , pp. 295-305
    • Schaller, H.1    Gondet, L.2    Maillot-Vernier, P.3    Benveniste, P.4
  • 26
    • 0000287651 scopus 로고
    • Inhibition of ergosterol biosynthesis in Saccharomyces cerevisiae and Ustilago maydis by tridemorph, tenpropimorph and fenpropidin
    • Baloch, R. I., Mercer, E. I., Wiggins, T. E. & Baldwin, B. C. (1984) Inhibition of ergosterol biosynthesis in Saccharomyces cerevisiae and Ustilago maydis by tridemorph, tenpropimorph and fenpropidin, Phytochemistry 23, 2219-2226.
    • (1984) Phytochemistry , vol.23 , pp. 2219-2226
    • Baloch, R.I.1    Mercer, E.I.2    Wiggins, T.E.3    Baldwin, B.C.4
  • 27
    • 37049120165 scopus 로고
    • Application of mass spectromelry to the structural investigation of 9,19-cyclosterols and triterpenes
    • Aplin, R. T. & Hornby, G. M. (1966) Application of mass spectromelry to the structural investigation of 9,19-cyclosterols and triterpenes, J. Chem. Soc. B, 1078-1079.
    • (1966) J. Chem. Soc. B , pp. 1078-1079
    • Aplin, R.T.1    Hornby, G.M.2
  • 28
    • 0039380421 scopus 로고
    • Effect of fenarimol on sterol biosynthesis in suspension cultures of bramble cells
    • Schmitt, P. & Benveniste, P. (1979) Effect of fenarimol on sterol biosynthesis in suspension cultures of bramble cells, Phytochemistry 18, 1659-1665.
    • (1979) Phytochemistry , vol.18 , pp. 1659-1665
    • Schmitt, P.1    Benveniste, P.2
  • 29
    • 0028357263 scopus 로고
    • Characterization of recombinant plant cinnamate 4-hydroxylase produced in yeast. Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway
    • Urban, P., Werck-Reichhart, D., Teutsch, H. G., Durst, F., Regnier, S., Kazmaier, M. & Pompon, D. (1994) Characterization of recombinant plant cinnamate 4-hydroxylase produced in yeast. Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway, Eur J. Biochem. 222, 843-850.
    • (1994) Eur J. Biochem. , vol.222 , pp. 843-850
    • Urban, P.1    Werck-Reichhart, D.2    Teutsch, H.G.3    Durst, F.4    Regnier, S.5    Kazmaier, M.6    Pompon, D.7
  • 30
    • 0028873790 scopus 로고
    • Sterol acyl transferase and steryl ester hydrolase activities in a tobacco mutant which overproduces sterols
    • Bouvier-Navé, P. & Benveniste, P. (1995) Sterol acyl transferase and steryl ester hydrolase activities in a tobacco mutant which overproduces sterols. Plant Sci. 110, 11-19.
    • (1995) Plant Sci. , vol.110 , pp. 11-19
    • Bouvier-Navé, P.1    Benveniste, P.2
  • 32
    • 0024348798 scopus 로고
    • The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol
    • Gaber, R. F., Copple, D. M., Kennedy, B. K., Vidal, M. & Bard, M. (1989) The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol. Mol. Cell. Biol. 9, 3447-3456.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3447-3456
    • Gaber, R.F.1    Copple, D.M.2    Kennedy, B.K.3    Vidal, M.4    Bard, M.5
  • 33
    • 0028355262 scopus 로고
    • SED6 is identical to ERG6, and encodes a putative methyltransferase required for ergosterol synthesis
    • Hardwick, K. G. & Pelham, H. R. B. (1994) SED6 is identical to ERG6, and encodes a putative methyltransferase required for ergosterol synthesis, Yeast 10, 265-269.
    • (1994) Yeast , vol.10 , pp. 265-269
    • Hardwick, K.G.1    Pelham, H.R.B.2
  • 34
    • 0029975946 scopus 로고    scopus 로고
    • Sterol specificity of the Saccharomyces cerevisiae ERG6 gene product expressed in Escherichia coli
    • Venkatramesh, M. & Nes, W. D. (1996) Sterol specificity of the Saccharomyces cerevisiae ERG6 gene product expressed in Escherichia coli, Lipids 31, 373-377.
    • (1996) Lipids , vol.31 , pp. 373-377
    • Venkatramesh, M.1    Nes, W.D.2
  • 35
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan, R. M. & Clarke, S. (1994) Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch. Biochem. Biophys. 310, 417-427.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 36
    • 0024398664 scopus 로고
    • Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA and small molecule S-adenosylmethionine-dependent methyltransferases
    • Ingrosso, D., Fowler, A. V., Bleibaum, J. & Clarke, S. (1989) Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA and small molecule S-adenosylmethionine-dependent methyltransferases. J. Biol. Chem. 264, 20131-20139.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20131-20139
    • Ingrosso, D.1    Fowler, A.V.2    Bleibaum, J.3    Clarke, S.4
  • 37
    • 0024216392 scopus 로고
    • The DNA and S-adenosylmethionine-binding regions of EcoDam and related methyltransferases
    • Guscheibauer, W. (1988) The DNA and S-adenosylmethionine-binding regions of EcoDam and related methyltransferases, Gene (Amst.) 74, 211-214.
    • (1988) Gene (Amst.) , vol.74 , pp. 211-214
    • Guscheibauer, W.1
  • 38
    • 0027674918 scopus 로고
    • Molecular cloning and expression of a new class of ortho-diphenol-O-methyltransferases induced in tobacco leaves by infection or elicitor treatment
    • Pellegrini, L. O. G., Geoffroy, P., Fritig, B. & Legrand, M. (1993) Molecular cloning and expression of a new class of ortho-diphenol-O-methyltransferases induced in tobacco leaves by infection or elicitor treatment. Plant Physiol. (Bethesda) 103, 509-517.
    • (1993) Plant Physiol. (Bethesda) , vol.103 , pp. 509-517
    • Pellegrini, L.O.G.1    Geoffroy, P.2    Fritig, B.3    Legrand, M.4
  • 39
    • 0028258821 scopus 로고
    • Cloning of a rat cDNA encoding dihydroxypolyprenylbenzoate methyltransferase by functional complementation of a Saccharomyces cerevisiae mutant deficient in ubiquinone biosynthesis
    • Marbois, B. H., Hsu, A., Pillai R., Colicelli, J. & Clarke, C. F. (1994) Cloning of a rat cDNA encoding dihydroxypolyprenylbenzoate methyltransferase by functional complementation of a Saccharomyces cerevisiae mutant deficient in ubiquinone biosynthesis, Gene (Amst.) 138, 213-217.
    • (1994) Gene (Amst.) , vol.138 , pp. 213-217
    • Marbois, B.H.1    Hsu, A.2    Pillai, R.3    Colicelli, J.4    Clarke, C.F.5
  • 40
    • 0025743250 scopus 로고
    • Cloning and disruption of the yeast C-8 sterol isomerase gene
    • Ashman, W. H., Barbuch, R. J., Ulbright, C. E., Jarrett, H. W. & Bard, M. (1991) Cloning and disruption of the yeast C-8 sterol isomerase gene, Lipids 26, 628-632.
    • (1991) Lipids , vol.26 , pp. 628-632
    • Ashman, W.H.1    Barbuch, R.J.2    Ulbright, C.E.3    Jarrett, H.W.4    Bard, M.5
  • 41
    • 0016012256 scopus 로고
    • Biosynthesis of terpenes and steroids. Part IX. The sterols of some mutant yeasts and their relationship to the biosynthesis of ergosterol
    • Barton, D. H. R., Corrie, J. E. T., Widdowson, D. A., Bard, M. & Woods, R. A. (1974) Biosynthesis of terpenes and steroids. Part IX. The sterols of some mutant yeasts and their relationship to the biosynthesis of ergosterol, J. Chem. Soc. Perkin I, 1326-1333.
    • (1974) J. Chem. Soc. Perkin I , pp. 1326-1333
    • Barton, D.H.R.1    Corrie, J.E.T.2    Widdowson, D.A.3    Bard, M.4    Woods, R.A.5
  • 42
    • 0001154042 scopus 로고
    • Sterol biosynthetic capability of purified membrane fractions from maize coleoptiles
    • Hartmann-Bouillon, M. A. & Benveniste, P. (1978) Sterol biosynthetic capability of purified membrane fractions from maize coleoptiles, Phytochemistry 17, 1037-1042.
    • (1978) Phytochemistry , vol.17 , pp. 1037-1042
    • Hartmann-Bouillon, M.A.1    Benveniste, P.2
  • 44
    • 0015932861 scopus 로고
    • Biosynthesis of ergosterol in yeast. Evidence for multiple pathways
    • Fryberg, M., Oehlschlager, A. C. & Unrau, A. M. (1973) Biosynthesis of ergosterol in yeast. Evidence for multiple pathways, J. Am. Chem. Soc. 95, 5747-5757.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 5747-5757
    • Fryberg, M.1    Oehlschlager, A.C.2    Unrau, A.M.3
  • 47
    • 0001525790 scopus 로고
    • Pecularities of sterol biosynthesis in plants
    • Ourisson, G. (1994) Pecularities of sterol biosynthesis in plants, J. Plant Physiol. 143, 434-439.
    • (1994) J. Plant Physiol. , vol.143 , pp. 434-439
    • Ourisson, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.