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Volumn 37, Issue 4, 1998, Pages 663-674

Conserved sequence motifs in plant S-adenosyl-L-methionine-dependent methyltransferases

Author keywords

CCoAOMT; Flavonoids; Methyltransferase; OMT; Phenylpropanoid; SAM

Indexed keywords

AMINO ACID SEQUENCE; COMPUTER ANALYSIS; ENZYME SPECIFICITY; FLAVONOID; METHYLTRANSFERASE; O METHYLTRANSFERASE; PHENYLPROPANOID; S ADENOSYLMETHIONINE;

EID: 0032126760     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006035210889     Document Type: Article
Times cited : (268)

References (24)
  • 1
    • 0030908496 scopus 로고    scopus 로고
    • Identification of cDNAs encoding sterol methyltransferases involved in the secondary methylation step of plant sterol biosynthesis
    • Bouvier-Nave P, Husselstein T, Desprez T, Benveniste P: Identification of cDNAs encoding sterol methyltransferases involved in the secondary methylation step of plant sterol biosynthesis. Eur J Biochem 246: 518-529 (1997).
    • (1997) Eur J Biochem , vol.246 , pp. 518-529
    • Bouvier-Nave, P.1    Husselstein, T.2    Desprez, T.3    Benveniste, P.4
  • 2
    • 0026409291 scopus 로고
    • cDNA cloning, sequence analysis and seasonal expression of lignin-bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase of aspen
    • Bugos RC, Chiang VL, Campbell WH: cDNA cloning, sequence analysis and seasonal expression of lignin-bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase of aspen. Plant Mol Biol 17: 1203-1215 (1991).
    • (1991) Plant Mol Biol , vol.17 , pp. 1203-1215
    • Bugos, R.C.1    Chiang, V.L.2    Campbell, W.H.3
  • 3
    • 7344220921 scopus 로고    scopus 로고
    • Isolation of tobacco cDNAs encoding caffeoyl-CoA 3-O-methyltransferase (accession no. Z56282 and Z82982)(PGR-039)
    • Busam G, Grimmig B, Knuesel RE, Matern U: Isolation of tobacco cDNAs encoding caffeoyl-CoA 3-O-methyltransferase (accession no. Z56282 and Z82982)(PGR-039) Plant Physiol 113: 1003 (1997).
    • (1997) Plant Physiol , vol.113 , pp. 1003
    • Busam, G.1    Grimmig, B.2    Knuesel, R.E.3    Matern, U.4
  • 4
    • 0029163078 scopus 로고
    • Structure and function of DNA methyltransferases
    • Cheng X: Structure and function of DNA methyltransferases. Annu Rev Biophys Biomol Struct 24: 293-318 (1995).
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 293-318
    • Cheng, X.1
  • 5
    • 0027338134 scopus 로고
    • Crystal structure of the HhaI DNA methyltransferase complexed with SAM
    • Cheng X, Kumar S, Posfai J, Pfugrath JW, Roberts RJ: Crystal structure of the HhaI DNA methyltransferase complexed with SAM. Cell 74: 299-307 (1993).
    • (1993) Cell , vol.74 , pp. 299-307
    • Cheng, X.1    Kumar, S.2    Posfai, J.3    Pfugrath, J.W.4    Roberts, R.J.5
  • 6
    • 0030157380 scopus 로고    scopus 로고
    • Phenylpropanoid metabolism and lignin biosynthesis: From weeds to trees
    • Douglass CJ: Phenylpropanoid metabolism and lignin biosynthesis: from weeds to trees. Trends Plant Sci 1: 171-179 (1996).
    • (1996) Trends Plant Sci , vol.1 , pp. 171-179
    • Douglass, C.J.1
  • 8
    • 0001341561 scopus 로고    scopus 로고
    • Plant OMT signatures
    • Ibrahim RK: Plant OMT signatures. Trends Plant Sci 2: 249-250 (1997).
    • (1997) Trends Plant Sci , vol.2 , pp. 249-250
    • Ibrahim, R.K.1
  • 9
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S adenosyl methionine dependent methyltransferases suggests a common structure for these enzymes
    • Kagan RM, Clarke S: Widespread occurrence of three sequence motifs in diverse S adenosyl methionine dependent methyltransferases suggests a common structure for these enzymes. Arch Biochem Biophys 310: 417-427 (1994).
    • (1994) Arch Biochem Biophys , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 10
    • 0024542208 scopus 로고
    • Evolution of type II methyltransferases
    • Lauster R: Evolution of type II methyltransferases. J Mol Biol 206: 313-321 (1989).
    • (1989) J Mol Biol , vol.206 , pp. 313-321
    • Lauster, R.1
  • 11
    • 0030973546 scopus 로고    scopus 로고
    • A novel multifunctional O-methyltransferase implicated in a dual methylation pathway associated with lignin biosynthesis in loblolly pine
    • Li L, Popko JL, Zhang XH, Osakabe K, Tsai CJ, Joshi CP, Chiang VL: A novel multifunctional O-methyltransferase implicated in a dual methylation pathway associated with lignin biosynthesis in loblolly pine. Proc Natl Acad Sci USA 94: 5461-5466 (1997).
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5461-5466
    • Li, L.1    Popko, J.L.2    Zhang, X.H.3    Osakabe, K.4    Tsai, C.J.5    Joshi, C.P.6    Chiang, V.L.7
  • 13
    • 0001276994 scopus 로고
    • Cloning of aspen (Populus tremuloides) xylem caffeoyl-CoA-3-O-methyltransferase (GenBank U27116)(PGR95-040)
    • Meng H, Campbell WH: Cloning of aspen (Populus tremuloides) xylem caffeoyl-CoA-3-O-methyltransferase (GenBank U27116)(PGR95-040). Plant Physiol 108: 1749 (1995).
    • (1995) Plant Physiol , vol.108 , pp. 1749
    • Meng, H.1    Campbell, W.H.2
  • 14
    • 0024688821 scopus 로고
    • S-Adenosyl-L-methionine: Trans-caffeoyl-coenzyme A 3-O-methyltransferase from elicitor-treated parsley cell suspension cultures
    • Pakusch A, Kneusel RE, Matern U: S-Adenosyl-L-methionine: trans-caffeoyl-coenzyme A 3-O-methyltransferase from elicitor-treated parsley cell suspension cultures. Arch Biochem Biophys 271: 488-494 (1989).
    • (1989) Arch Biochem Biophys , vol.271 , pp. 488-494
    • Pakusch, A.1    Kneusel, R.E.2    Matern, U.3
  • 15
    • 0027674918 scopus 로고
    • Molecular cloning and expression of a new class of O-diphenol-O-methyltransferases induced in tobacco (Nicotiana tabacum L.) leaves by infection or elicitor treatment
    • Pellegrini L, Geoffroy P, Fritig B, Legrand M: Molecular cloning and expression of a new class of O-diphenol-O-methyltransferases induced in tobacco (Nicotiana tabacum L.) leaves by infection or elicitor treatment. Plant Physiol 103: 509-517 (1993).
    • (1993) Plant Physiol , vol.103 , pp. 509-517
    • Pellegrini, L.1    Geoffroy, P.2    Fritig, B.3    Legrand, M.4
  • 16
    • 0024236266 scopus 로고    scopus 로고
    • Sequence motifs specific for cytosine methyltransferases
    • 19988
    • Posfai J, Bhagwat AS, Roberts RJ: Sequence motifs specific for cytosine methyltransferases. Gene 74: 261-265 (19988).
    • Gene , vol.74 , pp. 261-265
    • Posfai, J.1    Bhagwat, A.S.2    Roberts, R.J.3
  • 17
    • 0030295364 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA that encodes maize uroporphyrinogen III methyltransferase, an enzyme involved in the synthesis of siroheme, which is a prosthetic group of nitrite reductase
    • Sakakibara H, Takei K, Sugiyama T: Isolation and characterization of a cDNA that encodes maize uroporphyrinogen III methyltransferase, an enzyme involved in the synthesis of siroheme, which is a prosthetic group of nitrite reductase. Plant J 10: 883-892 (1996).
    • (1996) Plant J , vol.10 , pp. 883-892
    • Sakakibara, H.1    Takei, K.2    Sugiyama, T.3
  • 18
    • 0025948396 scopus 로고
    • Molecular cloning, induction, and taxonomic distribution of caffeoyl-CoA 3-O-methyltransferase, an enzyme involved in disease resistance
    • Schmitt D, Pakusch A-E, Matern U: Molecular cloning, induction, and taxonomic distribution of caffeoyl-CoA 3-O-methyltransferase, an enzyme involved in disease resistance. J Biol Chem 266, 17416-17423 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 17416-17423
    • Schmitt, D.1    Pakusch, A.-E.2    Matern, U.3
  • 19
    • 0026554141 scopus 로고
    • A novel methyltransferase induce by osmotic stress in the facultative halophyte Mesembryanthemum crystllinum
    • Vernon DM, Bohnert HJ: A novel methyltransferase induce by osmotic stress in the facultative halophyte Mesembryanthemum crystllinum. EMBO J 11: 2077-2085 (1992).
    • (1992) EMBO J , vol.11 , pp. 2077-2085
    • Vernon, D.M.1    Bohnert, H.J.2
  • 20
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren J, Svensson A, Liljas A: Crystal structure of catechol O-methyltransferase. Nature 368: 354-358 (1994).
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, A.2    Liljas, A.3
  • 21
    • 0028874074 scopus 로고
    • Lignin biosynthesis
    • Whetten R, Sederoff R: Lignin biosynthesis. Plant Cell 7: 1001-1013 (1995).
    • (1995) Plant Cell , vol.7 , pp. 1001-1013
    • Whetten, R.1    Sederoff, R.2
  • 22
    • 0026775096 scopus 로고
    • Isolation and characterization of E.coli mutants affected in aerobic respiration
    • Wu G, Williams HD, Zamanian M, Gibson F, Poole RK: Isolation and characterization of E.coli mutants affected in aerobic respiration. J Gen Microbiol 138: 2101-2112 (1992).
    • (1992) J Gen Microbiol , vol.138 , pp. 2101-2112
    • Wu, G.1    Williams, H.D.2    Zamanian, M.3    Gibson, F.4    Poole, R.K.5
  • 23
    • 0028520357 scopus 로고
    • An alternative methylation pathway in lignin biosynthesis in Zinnia
    • Ye Z-H, Kneusel RE, Matern U, Varner JE: An alternative methylation pathway in lignin biosynthesis in Zinnia. Plant Cell 6: 1427-1439 (1994).
    • (1994) Plant Cell , vol.6 , pp. 1427-1439
    • Ye, Z.-H.1    Kneusel, R.E.2    Matern, U.3    Varner, J.E.4
  • 24
    • 0030292845 scopus 로고    scopus 로고
    • Organization and characterization of the ribulose 1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase in tobacco
    • Ying Z, Janney N, Houtz RL: Organization and characterization of the ribulose 1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase in tobacco. Plant Mol Biol 32: 663-671 (1996).
    • (1996) Plant Mol Biol , vol.32 , pp. 663-671
    • Ying, Z.1    Janney, N.2    Houtz, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.