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Volumn 59, Issue 6, 2008, Pages 1383-1397

Structure-function analysis of the NB-ARC domain of plant disease resistance proteins

Author keywords

Intramolecular interactions; MHD motif; NB ARC domain; Plant disease resistance; Protein structure; R proteins; Signal transduction; Site directed mutagenesis

Indexed keywords

VEGETABLE PROTEIN;

EID: 45549084403     PISSN: 00220957     EISSN: 14602431     Source Type: Journal    
DOI: 10.1093/jxb/ern045     Document Type: Article
Times cited : (322)

References (47)
  • 3
    • 0035139202 scopus 로고    scopus 로고
    • Mutational analysis of the Arabidopsis RPS2 disease resistance gene and the corresponding Pseudomonas syringae avrRpt2 avirulence gene
    • Axtell MJ, McNellis TW, Mudgett MB, Hsu CS, Staskawicz BJ. 2001. Mutational analysis of the Arabidopsis RPS2 disease resistance gene and the corresponding Pseudomonas syringae avrRpt2 avirulence gene. Molecular Plant-Microbe Interactions 14, 181-188.
    • (2001) Molecular Plant-Microbe Interactions , vol.14 , pp. 181-188
    • Axtell, M.J.1    McNellis, T.W.2    Mudgett, M.B.3    Hsu, C.S.4    Staskawicz, B.J.5
  • 4
    • 0036775380 scopus 로고    scopus 로고
    • Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato
    • Bendahmane A, Farnham G, Moffett P, Baulcombe DC. 2002. Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato. The Plant Journal 32, 195-204.
    • (2002) The Plant Journal , vol.32 , pp. 195-204
    • Bendahmane, A.1    Farnham, G.2    Moffett, P.3    Baulcombe, D.C.4
  • 5
    • 35148827341 scopus 로고    scopus 로고
    • Elicitors, effectors, and R genes: The new paradigm and a lifetime supply of questions
    • Bent A, Mackey D. 2007. Elicitors, effectors, and R genes: the new paradigm and a lifetime supply of questions. Annual Review of Phytopathology 45, 399-436.
    • (2007) Annual Review of Phytopathology , vol.45 , pp. 399-436
    • Bent, A.1    Mackey, D.2
  • 7
    • 33846272114 scopus 로고    scopus 로고
    • Plant NBS-LRR proteins in pathogen sensing and host defense
    • DeYoung BJ, Innes RW. 2006. Plant NBS-LRR proteins in pathogen sensing and host defense. Nature Immunology 7, 1243-1249.
    • (2006) Nature Immunology , vol.7 , pp. 1243-1249
    • DeYoung, B.J.1    Innes, R.W.2
  • 9
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Research 32, 1792-1797.
    • (2004) Nucleic Acids Research , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 10
    • 33646888187 scopus 로고    scopus 로고
    • cDNA-AFLP combined with functional analysis reveals novel genes involved in the hypersensitive response
    • Gabriëls SHEJ, Takken FLW, Vossen JH, et al. 2006. cDNA-AFLP combined with functional analysis reveals novel genes involved in the hypersensitive response. Molecular Plant-Microbe Interactions 19, 567-576.
    • (2006) Molecular Plant-Microbe Interactions , vol.19 , pp. 567-576
    • Gabriëls, S.H.E.J.1    Takken, F.L.W.2    Vossen, J.H.3
  • 11
    • 33947711794 scopus 로고    scopus 로고
    • An NB-LRR protein required for HR signalling mediated by both extra- and intracellular resistance proteins
    • Gabriëls SHEJ, Vossen JH, Ekengren SK, et al. 2007. An NB-LRR protein required for HR signalling mediated by both extra- and intracellular resistance proteins. The Plant Journal 50, 14-28.
    • (2007) The Plant Journal , vol.50 , pp. 14-28
    • Gabriëls, S.H.E.J.1    Vossen, J.H.2    Ekengren, S.K.3
  • 13
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan KL, Dixon JE. 1991. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Analytical Biochemistry 192, 262-267.
    • (1991) Analytical Biochemistry , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 14
    • 0033771050 scopus 로고    scopus 로고
    • Technical focus: A guide to Agrobacterium binary Ti vectors
    • Hellens R, Mullineaux P, Klee H. 2000. Technical focus: a guide to Agrobacterium binary Ti vectors. Trends in Plant Science 5, 446-451.
    • (2000) Trends in Plant Science , vol.5 , pp. 446-451
    • Hellens, R.1    Mullineaux, P.2    Klee, H.3
  • 16
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R, Krummel B, Saiki RK. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Research 16, 7351-7367.
    • (1988) Nucleic Acids Research , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 17
    • 19544374693 scopus 로고    scopus 로고
    • Autoactive alleles of the flax L6 rust resistance gene induce non-race-specific rust resistance associated with the hypersensitive response
    • Howles P, Lawrence G, Finnegan J, McFadden H, Ayliffe M, Dodds P, Ellis J. 2005. Autoactive alleles of the flax L6 rust resistance gene induce non-race-specific rust resistance associated with the hypersensitive response. Molecular Plant-Microbe Interactions 18, 570-582.
    • (2005) Molecular Plant-Microbe Interactions , vol.18 , pp. 570-582
    • Howles, P.1    Lawrence, G.2    Finnegan, J.3    McFadden, H.4    Ayliffe, M.5    Dodds, P.6    Ellis, J.7
  • 18
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones JDG, Dangl JL. 2006. The plant immune system. Nature 444, 323-329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.G.1    Dangl, J.L.2
  • 19
    • 0030743251 scopus 로고    scopus 로고
    • Rapid and efficient site-directed mutagenesis by single-tube 'megaprimer' PCR method
    • Ke SH, Madison EL. 1997. Rapid and efficient site-directed mutagenesis by single-tube 'megaprimer' PCR method. Nucleic Acids Research 25, 3371-3372.
    • (1997) Nucleic Acids Research , vol.25 , pp. 3371-3372
    • Ke, S.H.1    Madison, E.L.2
  • 20
    • 0001200134 scopus 로고
    • The promoter of Tl-DNA gene 5 controls the tissue-specific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector
    • Koncz C, Schell J. 1986. The promoter of Tl-DNA gene 5 controls the tissue-specific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector. Molecular and General Genetics 204, 383-396.
    • (1986) Molecular and General Genetics , vol.204 , pp. 383-396
    • Koncz, C.1    Schell, J.2
  • 21
    • 4644247731 scopus 로고    scopus 로고
    • STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer
    • Leipe DD, Koonin EV, Aravind L. 2004. STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer. Journal of Molecular Biology 343, 1-28.
    • (2004) Journal of Molecular Biology , vol.343 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 24
    • 0033231602 scopus 로고    scopus 로고
    • Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily
    • Meyers BC, Dickerman AW, Michelmore RW, Sivaramakrishnan S, Sobral BW, Young ND. 1999. Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily. The Plant Journal 20, 317-332.
    • (1999) The Plant Journal , vol.20 , pp. 317-332
    • Meyers, B.C.1    Dickerman, A.W.2    Michelmore, R.W.3    Sivaramakrishnan, S.4    Sobral, B.W.5    Young, N.D.6
  • 25
    • 0037009437 scopus 로고    scopus 로고
    • Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death
    • Moffett P, Farnham G, Peart J, Baulcombe DC. 2002. Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death. EMBO Journal 21, 4511-4519.
    • (2002) EMBO Journal , vol.21 , pp. 4511-4519
    • Moffett, P.1    Farnham, G.2    Peart, J.3    Baulcombe, D.C.4
  • 26
    • 1642377971 scopus 로고    scopus 로고
    • Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    • Ogura T, Whiteheart SW, Wilkinson AJ. 2004. Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases. Journal of Structural Biology 146, 106-112.
    • (2004) Journal of Structural Biology , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 27
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T, Wilkinson AJ. 2001. AAA+ superfamily ATPases: common structure-diverse function. Genes Cells 6, 575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 28
    • 0034014008 scopus 로고    scopus 로고
    • Comparative genetics of nucleotide binding site-leucine rich repeat resistance gene homologues in the genomes of two dicotyledons: Tomato and Arabidopsis
    • Pan Q, Liu YS, Budai Hadrian O, Sela M, Carmel Goren L, Zamir D, Fluhr R. 2000. Comparative genetics of nucleotide binding site-leucine rich repeat resistance gene homologues in the genomes of two dicotyledons: tomato and Arabidopsis. Genetics 155, 309-322.
    • (2000) Genetics , vol.155 , pp. 309-322
    • Pan, Q.1    Liu, Y.S.2    Budai Hadrian, O.3    Sela, M.4    Carmel Goren, L.5    Zamir, D.6    Fluhr, R.7
  • 29
    • 20144382377 scopus 로고    scopus 로고
    • NRG1, a CC-NB-LRR protein, together with N, a TIR-NB-LRR protein, mediates resistance against Tobacco Mosaic Virus
    • Peart JR, Mestre P, Lu R, Malcuit I, Baulcombe DC. 2005. NRG1, a CC-NB-LRR protein, together with N, a TIR-NB-LRR protein, mediates resistance against Tobacco Mosaic Virus. Current Biology 15, 968-973.
    • (2005) Current Biology , vol.15 , pp. 968-973
    • Peart, J.R.1    Mestre, P.2    Lu, R.3    Malcuit, I.4    Baulcombe, D.C.5
  • 30
    • 33747473700 scopus 로고    scopus 로고
    • Distinct domains in the ARC region of the potato resistance protein Rx mediate LRR binding and inhibition of activation
    • Rairdan GJ, Moffett P. 2006. Distinct domains in the ARC region of the potato resistance protein Rx mediate LRR binding and inhibition of activation. The Plant Cell 18, 2082-2093.
    • (2006) The Plant Cell , vol.18 , pp. 2082-2093
    • Rairdan, G.J.1    Moffett, P.2
  • 31
    • 34247115054 scopus 로고    scopus 로고
    • Brothers in arms? Common and contrasting themes in pathogen perception by plant NB-LRR and animal NACHT-LRR proteins
    • Rairdan G, Moffett P. 2007. Brothers in arms? Common and contrasting themes in pathogen perception by plant NB-LRR and animal NACHT-LRR proteins. Microbes and Infection 9, 677-686.
    • (2007) Microbes and Infection , vol.9 , pp. 677-686
    • Rairdan, G.1    Moffett, P.2
  • 32
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl SJ, Li W, Chao Y, Schwarzenbacher R, Shi Y. 2005. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434, 926-933.
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 33
    • 1842430185 scopus 로고    scopus 로고
    • Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants
    • Rohila JS, Chen M, Cerny R, Fromm ME. 2004. Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. The Plant Journal 38, 172-181.
    • (2004) The Plant Journal , vol.38 , pp. 172-181
    • Rohila, J.S.1    Chen, M.2    Cerny, R.3    Fromm, M.E.4
  • 34
    • 0030581165 scopus 로고    scopus 로고
    • Tomato Prf is a member of the leucine-rich repeat class of plant disease resistance genes and lies embedded within the Pto kinase gene cluster
    • Salmeron JM, Oldroyd GED, Rommens CMT, Scofield SR, Kim HS, Lavelle DT, Dahlbeck D, Staskawicz BJ. 1996. Tomato Prf is a member of the leucine-rich repeat class of plant disease resistance genes and lies embedded within the Pto kinase gene cluster. Cell 86, 123-133.
    • (1996) Cell , vol.86 , pp. 123-133
    • Salmeron, J.M.1    Oldroyd, G.E.D.2    Rommens, C.M.T.3    Scofield, S.R.4    Kim, H.S.5    Lavelle, D.T.6    Dahlbeck, D.7    Staskawicz, B.J.8
  • 39
    • 0034489715 scopus 로고    scopus 로고
    • Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2
    • Tao Y, Yuan F, Leister RT, Ausubel FM, Katagiri F. 2000. Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2. The Plant Cell 12, 2541-2554.
    • (2000) The Plant Cell , vol.12 , pp. 2541-2554
    • Tao, Y.1    Yuan, F.2    Leister, R.T.3    Ausubel, F.M.4    Katagiri, F.5
  • 41
    • 0036009775 scopus 로고    scopus 로고
    • Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein
    • Tornero P, Chao RA, Luthin WN, Goff SA, Dangl JL. 2002. Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein. The Plant Cell 14, 435-450.
    • (2002) The Plant Cell , vol.14 , pp. 435-450
    • Tornero, P.1    Chao, R.A.2    Luthin, W.N.3    Goff, S.A.4    Dangl, J.L.5
  • 42
    • 0032568168 scopus 로고    scopus 로고
    • The NB-ARC domain: A novel signalling motif shared by plant resistance gene products and regulators of cell death in animals
    • van der Biezen EA, Jones JDG. 1998. The NB-ARC domain: a novel signalling motif shared by plant resistance gene products and regulators of cell death in animals. Current Biology 8, R226-R228.
    • (1998) Current Biology , vol.8
    • van der Biezen, E.A.1    Jones, J.D.G.2
  • 45
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. 1990. WHAT IF: a molecular modeling and drug design program. Journal of Molecular Graphics 8, 52-56.
    • (1990) Journal of Molecular Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 46
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan N, Chai J, Lee ES, et al. 2005. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437, 831-837.
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1    Chai, J.2    Lee, E.S.3
  • 47
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Ye Y, Godzik A. 2003. Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 19, Supplement 2, II246-II255.
    • (2003) Bioinformatics , vol.19 , Issue.SUPPL.EMENT 2
    • Ye, Y.1    Godzik, A.2


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