메뉴 건너뛰기




Volumn 108, Issue 14, 2011, Pages 5897-5902

Adaptive evolution of threonine deaminase in plant defense against insect herbivores

Author keywords

Induced resistance; Jasmonate; Molecular evolution; Plant insect interaction; Protein stability

Indexed keywords

2 OXOBUTYRIC ACID; AMMONIA; ISOENZYME; ISOLEUCINE; THREONINE DEHYDRATASE;

EID: 79955012413     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1016157108     Document Type: Article
Times cited : (66)

References (39)
  • 1
    • 0000651050 scopus 로고
    • Butterflies and plants: A study in coevolution
    • Ehrlich PR, Raven PH (1964) Butterflies and plants: A study in coevolution. Evolution 18:586-608.
    • (1964) Evolution , vol.18 , pp. 586-608
    • Ehrlich, P.R.1    Raven, P.H.2
  • 2
    • 48949120144 scopus 로고    scopus 로고
    • Facing the future of plant-insect interaction research: Le retour à la "raison d'être"
    • DOI 10.1104/pp.107.113472
    • Berenbaum MR, Zangerl AR (2008) Facing the future of plant-insect interaction research: Le retour à la "raison d'être". Plant Physiol 146:804-811. (Pubitemid 352844093)
    • (2008) Plant Physiology , vol.146 , Issue.3 , pp. 804-811
    • Berenbaum, M.R.1    Zanger, A.R.2
  • 3
    • 0242699693 scopus 로고
    • The raison d'être of secondary plant substances; These odd chemicals arose as a means of protecting plants from insects and now guide insects to food
    • Fraenkel GS (1959) The raison d'être of secondary plant substances; these odd chemicals arose as a means of protecting plants from insects and now guide insects to food. Science 129:1466-1470.
    • (1959) Science , vol.129 , pp. 1466-1470
    • Fraenkel, G.S.1
  • 4
    • 44449179468 scopus 로고    scopus 로고
    • Plant immunity to insect herbivores
    • DOI 10.1146/annurev.arplant.59.032607.092825
    • Howe GA, Jander G (2008) Plant immunity to insect herbivores. Annu Rev Plant Biol 59:41-66. (Pubitemid 351813023)
    • (2008) Annual Review of Plant Biology , vol.59 , pp. 41-66
    • Howe, G.A.1    Jander, G.2
  • 5
    • 48949120136 scopus 로고    scopus 로고
    • Arthropod-inducible proteins: Broad spectrum defenses against multiple herbivores
    • DOI 10.1104/pp.107.112177
    • Zhu-Salzman K, Luthe DS, Felton GW (2008) Arthropod-inducible proteins: Broad spectrum defenses against multiple herbivores. Plant Physiol 146:852-858. (Pubitemid 352844100)
    • (2008) Plant Physiology , vol.146 , Issue.3 , pp. 852-858
    • Zhu-Salzman, K.1    Luthe, D.S.2    Felton, G.W.3
  • 6
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan CA (1990) Protease inhibitors in plants: Genes for improving defenses against insects and pathogens. Annu Rev Phytopathol 28:425-449.
    • (1990) Annu Rev Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 7
    • 0000698945 scopus 로고
    • Herbivory in relation to plant nitrogen content
    • Mattson WJ (1980) Herbivory in relation to plant nitrogen content. Annu Rev Ecol Syst 11:119-161.
    • (1980) Annu Rev Ecol Syst , vol.11 , pp. 119-161
    • Mattson, W.J.1
  • 10
    • 0343070062 scopus 로고
    • Isoleucine-requiring Nicotiana plant deficient in threonine deaminase
    • Sidorov V, Menczel L, Maliga P (1981) Isoleucine-requiring Nicotiana plant deficient in threonine deaminase. Nature 294:87-88.
    • (1981) Nature , vol.294 , pp. 87-88
    • Sidorov, V.1    Menczel, L.2    Maliga, P.3
  • 11
    • 33845803150 scopus 로고    scopus 로고
    • Silencing threonine deaminase and JAR4 in Nicotiana attenuata impairs jasmonic acid-isoleucine-mediated defenses against Manduca sexta
    • DOI 10.1105/tpc.106.041103
    • Kang JH, Wang L, Giri A, Baldwin IT (2006) Silencing threonine deaminase and JAR4 in Nicotiana attenuata impairs jasmonic acid-isoleucine-mediated defenses against Manduca sexta. Plant Cell 18:3303-3320. (Pubitemid 46013292)
    • (2006) Plant Cell , vol.18 , Issue.11 , pp. 3303-3320
    • Kang, J.-H.1    Wang, L.2    Giri, A.3    Baldwin, I.T.4
  • 12
    • 0842291761 scopus 로고    scopus 로고
    • The Tomato Homolog of Coronatine-Insensitive1 Is Required for the Maternal Control of Seed Maturation, Jasmonate-Signaled Defense Responses, and Glandular Trichome Development
    • DOI 10.1105/tpc.017954
    • Li L, et al. (2004) The tomato homolog of CORONATINE-INSENSITIVE1 is required for the maternal control of seed maturation, jasmonate-signaled defense responses, and glandular trichome development. Plant Cell 16:126-143. (Pubitemid 38162358)
    • (2004) Plant Cell , vol.16 , Issue.1 , pp. 126-143
    • Li, L.1    Zhao, Y.2    McCaig, B.C.3    Wingerd, B.A.4    Wang, J.5    Whalon, M.E.6    Pichersky, E.7    Howe, G.A.8
  • 13
    • 34249780833 scopus 로고    scopus 로고
    • Stability of plant defense proteins in the gut of insect herbivores
    • DOI 10.1104/pp.107.095588
    • Chen H, Gonzales-Vigil E, Wilkerson CG, Howe GA (2007) Stability of plant defense proteins in the gut of insect herbivores. Plant Physiol 143:1954-1967. (Pubitemid 46849501)
    • (2007) Plant Physiology , vol.143 , Issue.4 , pp. 1954-1967
    • Chen, H.1    Gonzales-Vigil, E.2    Wilkerson, C.G.3    Howe, G.A.4
  • 14
    • 0026918137 scopus 로고
    • General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding
    • Hildmann T, et al. (1992) General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. Plant Cell 4:1157-1170.
    • (1992) Plant Cell , vol.4 , pp. 1157-1170
    • Hildmann, T.1
  • 15
    • 0028979329 scopus 로고
    • Expression of an amino acid biosynthesis gene in tomato flowers: Developmental upregulation and MeJa response are parenchyma-specific and mutually compatible
    • Samach A, Broday L, Hareven D, Lifschitz E (1995) Expression of an amino acid biosynthesis gene in tomato flowers: Developmental upregulation and MeJa response are parenchyma-specific and mutually compatible. Plant J 8:391-406.
    • (1995) Plant J , vol.8 , pp. 391-406
    • Samach, A.1    Broday, L.2    Hareven, D.3    Lifschitz, E.4
  • 16
    • 0031260101 scopus 로고    scopus 로고
    • The adaptation of insects to plant protease inhibitors
    • DOI 10.1016/S0022-1910(97)00040-1, PII S0022191097000401
    • Bolter C, Jongsma MA (1997) The adaptation of insects to plant protease inhibitors. J Insect Physiol 43:885-895. (Pubitemid 27521869)
    • (1997) Journal of Insect Physiology , vol.43 , Issue.10 , pp. 885-895
    • Jongsma, M.A.1    Bolter, C.2
  • 17
    • 0034642216 scopus 로고    scopus 로고
    • Evidence for two distinct effectorbinding sites in threonine deaminase by site-directed mutagenesis, kinetic, and binding experiments
    • Wessel PM, Graciet E, Douce R, Dumas R (2000) Evidence for two distinct effectorbinding sites in threonine deaminase by site-directed mutagenesis, kinetic, and binding experiments. Biochemistry 39:15136-15143.
    • (2000) Biochemistry , vol.39 , pp. 15136-15143
    • Wessel, P.M.1    Graciet, E.2    Douce, R.3    Dumas, R.4
  • 18
    • 33845991866 scopus 로고    scopus 로고
    • Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation
    • DOI 10.1074/jbc.M605721200
    • Simanshu DK, Savithri HS, Murthy MRN (2006) Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation. J Biol Chem 281:39630-39641. (Pubitemid 46041922)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39630-39641
    • Simanshu, D.K.1    Savithri, H.S.2    Murthy, M.R.N.3
  • 19
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • DOI 10.1074/jbc.M401865200
    • Bae E, Phillips GN, Jr (2004) Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J Biol Chem 279:28202-28208. (Pubitemid 38900096)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28202-28208
    • Bae, E.1    Phillips Jr., G.N.2
  • 20
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • DOI 10.1016/S0969-2126(00)00133-7
    • Szilágyi A, Závodszky P (2000) Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey. Structure 8:493-504. (Pubitemid 30304547)
    • (2000) Structure , vol.8 , Issue.5 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 22
    • 0029769692 scopus 로고    scopus 로고
    • The probability of attack and patterns of constitutive and induced defense: A test of optimal defense theory
    • Zangerl AR, Rutledge CE (1996) The probability of attack and patterns of constitutive and induced defense: A test of optimal defense theory. Am Nat 147:599-608.
    • (1996) Am Nat , vol.147 , pp. 599-608
    • Zangerl, A.R.1    Rutledge, C.E.2
  • 23
    • 33749399830 scopus 로고    scopus 로고
    • Structural and functional diversities in lepidopteran serine proteases
    • DOI 10.2478/s11658-006-0012-8
    • Srinivasan A, Giri AP, Gupta VS (2006) Structural and functional diversities in lepidopteran serine proteases. Cell Mol Biol Lett 11:132-154. (Pubitemid 44504052)
    • (2006) Cellular and Molecular Biology Letters , vol.11 , Issue.1 , pp. 132-154
    • Srinivasan, A.1    Giri, A.P.2    Gupta, V.S.3
  • 24
    • 0000316764 scopus 로고    scopus 로고
    • Characterization and Distribution of Chymotrypsin-Like and Other Digestive Proteases in Colorado Potato Beetle Larvae
    • Novillo C, Castanera P, Ortego F (1997) Characterization and distribution of chymotrypsin-like and other digestive proteases in Colorado potato beetle larvae. Arch Insect Biochem Physiol 36:181-201. (Pubitemid 127439910)
    • (1997) Archives of Insect Biochemistry and Physiology , vol.36 , Issue.3 , pp. 181-201
    • Novillo, C.1    Castanera, P.2    Ortego, F.3
  • 25
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • DOI 10.1128/MMBR.65.1.1-43.2001
    • Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43. (Pubitemid 32204286)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 26
    • 77955935755 scopus 로고    scopus 로고
    • Gene duplications and the time thereafter-examples from plant secondary metabolism
    • Ober D (2010) Gene duplications and the time thereafter-examples from plant secondary metabolism. Plant Biol (Stuttg) 12:570-577.
    • (2010) Plant Biol (Stuttg) , vol.12 , pp. 570-577
    • Ober, D.1
  • 27
    • 49649114289 scopus 로고    scopus 로고
    • Escape from adaptive conflict after duplication in an anthocyanin pathway gene
    • Des Marais DL, Rausher MD (2008) Escape from adaptive conflict after duplication in an anthocyanin pathway gene. Nature 454:762-765.
    • (2008) Nature , vol.454 , pp. 762-765
    • Des Marais, D.L.1    Rausher, M.D.2
  • 28
    • 77954743785 scopus 로고    scopus 로고
    • Mutational effects and the evolution of new protein functions
    • Soskine M, Tawfik DS (2010) Mutational effects and the evolution of new protein functions. Nat Rev Genet 11:572-582.
    • (2010) Nat Rev Genet , vol.11 , pp. 572-582
    • Soskine, M.1    Tawfik, D.S.2
  • 29
    • 34247185391 scopus 로고    scopus 로고
    • Functional diversification of acyl-coenzyme A oxidases in jasmonic acid biosynthesis and action
    • DOI 10.1104/pp.106.092916
    • Schilmiller AL, Koo AJK, Howe GA (2007) Functional diversification of acyl-coenzyme A oxidases in jasmonic acid biosynthesis and action. Plant Physiol 143:812-824. (Pubitemid 46940975)
    • (2007) Plant Physiology , vol.143 , Issue.2 , pp. 812-824
    • Schilmiller, A.L.1    Koo, A.J.K.2    Howe, G.A.3
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A (1997) MOLREP: An automated program for molecular replacement. J Appl Cryst 30:1022-1025. (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 34
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Calpha geometry: Phi, psi and Cbeta deviation
    • Lovell SC, et al. (2003) Structure validation by Calpha geometry: Phi, psi and Cbeta deviation. Proteins 50:437-450.
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1
  • 35
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL workspace: A webbased environment for protein structure homology modelling. Bioinformatics 22: 195-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 36
    • 0030442990 scopus 로고    scopus 로고
    • Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures
    • DOI 10.1002/(SICI)1097-0134(199612)26:4<363::AID-PROT1>3.0.CO;2-D
    • Hooft RWW, Sander C, Vriend G (1996) Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. Proteins 26:363-376. (Pubitemid 27024754)
    • (1996) Proteins: Structure, Function and Genetics , vol.26 , Issue.4 , pp. 363-376
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 38
    • 0025398721 scopus 로고
    • WHAT IF. A molecular modeling and drug design program
    • DOI 10.1016/0263-7855(90)80070-V
    • Vriend G (1990) WHAT IF: A molecular modeling and drug design program. J Mol Graphics 8:52-56. (Pubitemid 20717037)
    • (1990) Journal of Molecular Graphics , vol.8 , Issue.1 , pp. 52-56
    • Vriend, G.1
  • 39
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372:774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.