메뉴 건너뛰기




Volumn 227, Issue 3, 2008, Pages 517-526

Identification of the OsOPR7 gene encoding 12-oxophytodienoate reductase involved in the biosynthesis of jasmonic acid in rice

Author keywords

12 Oxophytodienoate reductase; Jasmonic acid; Oryza; Rice

Indexed keywords

12 OXOPHYTODIENOATE REDUCTASE; 12-OXOPHYTODIENOATE REDUCTASE; ARABIDOPSIS PROTEIN; CYCLOPENTANE DERIVATIVE; JASMONIC ACID; OPR3 PROTEIN, ARABIDOPSIS; OXIDOREDUCTASE; OXYLIPIN; UNCLASSIFIED DRUG; WATER;

EID: 38049008087     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-007-0635-7     Document Type: Article
Times cited : (131)

References (40)
  • 1
    • 0141996363 scopus 로고    scopus 로고
    • Diverse environmental cues transiently regulate OsOPR1 of the "octadecanoid pathway" revealing its importance in rice defense/stress and development
    • Agrawal GK, Jwa NS, Shibato J, Han O, Iwahashi H, Rakwal R (2003) Diverse environmental cues transiently regulate OsOPR1 of the "octadecanoid pathway" revealing its importance in rice defense/stress and development. Biochem Biophys Res Commun 310:1073-1082
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 1073-1082
    • Agrawal, G.K.1    Jwa, N.S.2    Shibato, J.3    Han, O.4    Iwahashi, H.5    Rakwal, R.6
  • 2
    • 0030187450 scopus 로고    scopus 로고
    • Strong, constitutive expression of the Arabidopsis ACT2/ACT8 actin subclass in vegetative tissues
    • An YQ, McDowell JM, Huang S, McKinney EC, Chambliss S, Meagher RB (1996) Strong, constitutive expression of the Arabidopsis ACT2/ACT8 actin subclass in vegetative tissues. Plant J 10:107-121
    • (1996) Plant J , vol.10 , pp. 107-121
    • An, Y.Q.1    McDowell, J.M.2    Huang, S.3    McKinney, E.C.4    Chambliss, S.5    Meagher, R.B.6
  • 3
    • 0034980393 scopus 로고    scopus 로고
    • X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE
    • Breithaupt C, Strassner J, Breitinger U, Huber R, Macheroux P, Schaller A, Clausen T (2001) X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. Structure 9:419-429
    • (2001) Structure , vol.9 , pp. 419-429
    • Breithaupt, C.1    Strassner, J.2    Breitinger, U.3    Huber, R.4    MacHeroux, P.5    Schaller, A.6    Clausen, T.7
  • 6
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16:735-743
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 7
    • 0002262342 scopus 로고
    • Volatile products of the lipoxygenase pathway evolved from Phaseolus vulgaris (L.) leaves inoculated with Pseudomonas syringae pv phaseolicola
    • Croft K, Juttner F, Slusarenko AJ (1993) Volatile products of the lipoxygenase pathway evolved from Phaseolus vulgaris (L.) leaves inoculated with Pseudomonas syringae pv phaseolicola. Plant Physiol 101:13-24
    • (1993) Plant Physiol , vol.101 , pp. 13-24
    • Croft, K.1    Juttner, F.2    Slusarenko, A.J.3
  • 8
    • 0041569777 scopus 로고    scopus 로고
    • Jasmonates and related oxylipins in plant responses to pathogenesis and herbivory
    • Farmer EE, Almeras E, Krishnamurthy V (2003) Jasmonates and related oxylipins in plant responses to pathogenesis and herbivory. Curr Opin Plant Biol 6:372-378
    • (2003) Curr Opin Plant Biol , vol.6 , pp. 372-378
    • Farmer, E.E.1    Almeras, E.2    Krishnamurthy, V.3
  • 9
    • 0024076281 scopus 로고
    • Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins
    • Gould SJ, Keller GA, Subramani S (1988) Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins. J Cell Biol 107:897-905
    • (1988) J Cell Biol , vol.107 , pp. 897-905
    • Gould, S.J.1    Keller, G.A.2    Subramani, S.3
  • 11
    • 0031569411 scopus 로고    scopus 로고
    • Analysis of 12-oxo-phytodienoic acid enantiomers in biological samples by capillary gas chromatography-mass spectrometry using cyclodextrin stationary phases
    • Laudert D, Hennig P, Stelmach BA, Muller A, Andert L, Weiler EW (1997) Analysis of 12-oxo-phytodienoic acid enantiomers in biological samples by capillary gas chromatography-mass spectrometry using cyclodextrin stationary phases. Anal Biochem 246:211-217
    • (1997) Anal Biochem , vol.246 , pp. 211-217
    • Laudert, D.1    Hennig, P.2    Stelmach, B.A.3    Muller, A.4    Andert, L.5    Weiler, E.W.6
  • 13
    • 0037016701 scopus 로고    scopus 로고
    • Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty acid hydroperoxides for aliphatic aldehyde production
    • Leon J, Royo J, Vancanneyt G, Sanz C, Silkowski H, Griffiths G, Sanchez-Serrano JJ (2002) Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty acid hydroperoxides for aliphatic aldehyde production. J Biol Chem 277:416-423
    • (2002) J Biol Chem , vol.277 , pp. 416-423
    • Leon, J.1    Royo, J.2    Vancanneyt, G.3    Sanz, C.4    Silkowski, H.5    Griffiths, G.6    Sanchez-Serrano, J.J.7
  • 14
    • 3142656622 scopus 로고    scopus 로고
    • JASMONATE-INSENSITIVE1 encodes a MYC transcription factor essential to discriminate between different jasmonate-regulated defense responses in Arabidopsis
    • Lorenzo O, Chico JM, Sanchez-Serrano JJ, Sorano R (2004) JASMONATE-INSENSITIVE1 encodes a MYC transcription factor essential to discriminate between different jasmonate-regulated defense responses in Arabidopsis. Plant Cell 16:1938-1950
    • (2004) Plant Cell , vol.16 , pp. 1938-1950
    • Lorenzo, O.1    Chico, J.M.2    Sanchez-Serrano, J.J.3    Sorano, R.4
  • 15
    • 0036010197 scopus 로고    scopus 로고
    • Distribution and characterization of peroxisomes in Arabidopsis by visualization with GFP: Dynamic morphology and actin-dependent movement
    • Mano S, Nakamori C, Hayashi M, Kato A, Kondo M, Nishimura M (2002) Distribution and characterization of peroxisomes in Arabidopsis by visualization with GFP: dynamic morphology and actin-dependent movement. Plant Cell Physiol 43:331-341
    • (2002) Plant Cell Physiol , vol.43 , pp. 331-341
    • Mano, S.1    Nakamori, C.2    Hayashi, M.3    Kato, A.4    Kondo, M.5    Nishimura, M.6
  • 16
    • 0034090616 scopus 로고    scopus 로고
    • Allene oxide synthases of barley (Hordeum vulgare cv. Salome): Tissue specific regulation in seedling development
    • Maucher H, Hause B, Feussner I, Ziegler J, Wasternack C (2000) Allene oxide synthases of barley (Hordeum vulgare cv. Salome): tissue specific regulation in seedling development. Plant J 21:199-213
    • (2000) Plant J , vol.21 , pp. 199-213
    • Maucher, H.1    Hause, B.2    Feussner, I.3    Ziegler, J.4    Wasternack, C.5
  • 21
    • 0035095841 scopus 로고    scopus 로고
    • Enzymes of the biosynthesis of octadecanoid-derived signalling molecules
    • Schaller F (2001) Enzymes of the biosynthesis of octadecanoid-derived signalling molecules. J Exp Bot 52:11-23
    • (2001) J Exp Bot , vol.52 , pp. 11-23
    • Schaller, F.1
  • 22
    • 0030974941 scopus 로고    scopus 로고
    • Enzymes of octadecanoid biosynthesis in plants-12-oxo-phytodienoate 10,11-reductase
    • Schaller F, Weiler EW (1997a) Enzymes of octadecanoid biosynthesis in plants-12-oxo-phytodienoate 10,11-reductase. Eur J Biochem 245:294-299
    • (1997) Eur J Biochem , vol.245 , pp. 294-299
    • Schaller, F.1    Weiler, E.W.2
  • 23
    • 0030869796 scopus 로고    scopus 로고
    • Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana. Structural and functional relationship to yeast old yellow enzyme
    • Schaller F, Weiler EW (1997b) Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana. Structural and functional relationship to yeast old yellow enzyme. J Biol Chem 272:28066-28072
    • (1997) J Biol Chem , vol.272 , pp. 28066-28072
    • Schaller, F.1    Weiler, E.W.2
  • 24
    • 0034031727 scopus 로고    scopus 로고
    • 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis
    • Schaller F, Biesgen C, Mussig C, Altmann T, Weiler EW (2000) 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis. Planta 210:979-984
    • (2000) Planta , vol.210 , pp. 979-984
    • Schaller, F.1    Biesgen, C.2    Mussig, C.3    Altmann, T.4    Weiler, E.W.5
  • 25
    • 20444480631 scopus 로고    scopus 로고
    • Systemic signaling in the wound response
    • Review
    • Schilmiller AL, Howe GA (2005) Systemic signaling in the wound response. Curr Opin Plant Biol 8:369-377 Review
    • (2005) Curr Opin Plant Biol , vol.8 , pp. 369-377
    • Schilmiller, A.L.1    Howe, G.A.2
  • 27
    • 0028854707 scopus 로고
    • Allene oxide synthase and allene oxide cyclase, enzymes of the jasmonic acid pathway, localized in Glycine max tissues
    • Simpson TD, Gardner HW (1995) Allene oxide synthase and allene oxide cyclase, enzymes of the jasmonic acid pathway, localized in Glycine max tissues. Plant Physiol 108:199-202
    • (1995) Plant Physiol , vol.108 , pp. 199-202
    • Simpson, T.D.1    Gardner, H.W.2
  • 29
    • 4043089251 scopus 로고    scopus 로고
    • The oxylipin signal jasmonic acid is activated by an enzyme that conjugates it to isoleucine in Arabidopsis
    • Staswick PE, Tiryaki I (2004) The oxylipin signal jasmonic acid is activated by an enzyme that conjugates it to isoleucine in Arabidopsis. Plant Cell 16:2117-2127
    • (2004) Plant Cell , vol.16 , pp. 2117-2127
    • Staswick, P.E.1    Tiryaki, I.2
  • 30
    • 0034641758 scopus 로고    scopus 로고
    • The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis
    • Stintzi A, Browse J (2000) The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis. Proc Natl Acad Sci USA 97:10625-10630
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10625-10630
    • Stintzi, A.1    Browse, J.2
  • 31
    • 0041031592 scopus 로고    scopus 로고
    • A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein
    • Strassner J, Furholz A, Macheroux P, Amrhein N, Schaller A (1999) A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein. J Biol Chem 274:35067-35073
    • (1999) J Biol Chem , vol.274 , pp. 35067-35073
    • Strassner, J.1    Furholz, A.2    MacHeroux, P.3    Amrhein, N.4    Schaller, A.5
  • 32
    • 0010632418 scopus 로고    scopus 로고
    • Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response
    • Strassner J, Schaller F, Frick UB, Howe GA, Weiler EW, Amrhein N, Macheroux P, Schaller A (2002) Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response. Plant J 32:585-601
    • (2002) Plant J , vol.32 , pp. 585-601
    • Strassner, J.1    Schaller, F.2    Frick, U.B.3    Howe, G.A.4    Weiler, E.W.5    Amrhein, N.6    MacHeroux, P.7    Schaller, A.8
  • 35
    • 0038167906 scopus 로고    scopus 로고
    • Efficient synthesis of the OPC homologous series, OPC-1:0, -3:0, -4:0, -5:0, -6:0, -7:0, and -8:0
    • Toshima H, Nara S, Aramaki H, Ichihara A, Koda Y, Kikuta Y (1997) Efficient synthesis of the OPC homologous series, OPC-1:0, -3:0, -4:0, -5:0, -6:0, -7:0, and -8:0. Biosci Biotechnol Biochem 61:1724-1728
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1724-1728
    • Toshima, H.1    Nara, S.2    Aramaki, H.3    Ichihara, A.4    Koda, Y.5    Kikuta, Y.6
  • 37
    • 0001699831 scopus 로고
    • Biosynthesis of jasmonic acid by several plant species
    • Vick BA, Zimmerman DC (1984) Biosynthesis of jasmonic acid by several plant species. Plant Physiol 75:458-461
    • (1984) Plant Physiol , vol.75 , pp. 458-461
    • Vick, B.A.1    Zimmerman, D.C.2
  • 38
    • 0034543482 scopus 로고    scopus 로고
    • Fatty acid ketodienes and fatty acid ketotrienes: Michael addition acceptors that accumulate in wounded and diseased Arabidopsis leaves
    • Vollenweider S, Weber H, Stolz S, Chetelat A, Farmer EE (2000) Fatty acid ketodienes and fatty acid ketotrienes: Michael addition acceptors that accumulate in wounded and diseased Arabidopsis leaves. Plant J 24:467-476
    • (2000) Plant J , vol.24 , pp. 467-476
    • Vollenweider, S.1    Weber, H.2    Stolz, S.3    Chetelat, A.4    Farmer, E.E.5
  • 39
    • 0032524404 scopus 로고    scopus 로고
    • COI1: An Arabidopsis gene required for jasmonate-regulated defense and fertility
    • Xie DX, Feys BF, James S, Nieto-Rostro M, Turner JG (1998) COI1: an Arabidopsis gene required for jasmonate-regulated defense and fertility. Science 280:1091-1094
    • (1998) Science , vol.280 , pp. 1091-1094
    • Xie, D.X.1    Feys, B.F.2    James, S.3    Nieto-Rostro, M.4    Turner, J.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.