메뉴 건너뛰기




Volumn 50, Issue 6, 2007, Pages 1107-1117

Purification of the M flax-rust resistance protein expressed in Pichia pastoris

Author keywords

Disease resistance; Flax; Pichia pastoris; Recombinant protein; TIR NBS LRR

Indexed keywords

DISEASES; GENETIC ENGINEERING; PLANTS (BOTANY);

EID: 34250159521     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2007.03104.x     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 0002624023 scopus 로고
    • Molecular sieve methods of analysis
    • In. Vol. 1 (. Neurath, H. Hill, R.L. eds). New York: Academic press, pp.
    • Ackers, G.K. (1976) Molecular sieve methods of analysis. In The Proteins, Vol. 1 (Neurath, H. Hill, R.L. eds). New York : Academic press, pp. 1 94.
    • (1976) The Proteins , pp. 1-94
    • Ackers, G.K.1
  • 2
    • 21444455218 scopus 로고    scopus 로고
    • RIN13 is a positive regulator of the plant disease resistance protein RPM1
    • Al-Daoude, A., Zabala, M.D., Ko, J.H. Grant, M. (2005) RIN13 is a positive regulator of the plant disease resistance protein RPM1. Plant Cell, 17, 1016 28.
    • (2005) Plant Cell , vol.17 , pp. 1016-28
    • Al-Daoude, A.1    Zabala, M.D.2    Ko, J.H.3    Grant, M.4
  • 3
    • 0031127301 scopus 로고    scopus 로고
    • Inactivation of the flax rust resistance gene M associated with loss of a repeated unit within the leucine-rich repeat coding region
    • Anderson, P.A., Lawrence, G.J., Morrish, B.C., Ayliffe, M.A., Finnegan, E.J. Ellis, J.G. (1997) Inactivation of the flax rust resistance gene M associated with loss of a repeated unit within the leucine-rich repeat coding region. Plant Cell, 9, 641 51.
    • (1997) Plant Cell , vol.9 , pp. 641-51
    • Anderson, P.A.1    Lawrence, G.J.2    Morrish, B.C.3    Ayliffe, M.A.4    Finnegan, E.J.5    Ellis, J.G.6
  • 4
    • 10344257928 scopus 로고    scopus 로고
    • Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream or independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial Type III effectors AvrRpt2 or AvrRpm1
    • Belkhadir, Y., Nimchuk, Z., Hubert, D.A., Mackey, D. Dangl, J.L. (2004) Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream or independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial Type III effectors AvrRpt2 or AvrRpm1. Plant Cell, 16, 2822 35.
    • (2004) Plant Cell , vol.16 , pp. 2822-35
    • Belkhadir, Y.1    Nimchuk, Z.2    Hubert, D.A.3    MacKey, D.4    Dangl, J.L.5
  • 5
    • 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, D.C. (2002) Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato. Plant J. 32, 195 204.
    • (2002) Plant J. , vol.32 , pp. 195-204
    • Bendahmane, A.1    Farnham, G.2    Moffett, P.3    Baulcombe, D.C.4
  • 6
    • 0036008975 scopus 로고    scopus 로고
    • Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR genes and confers downy mildew resistance through multiple signalling components
    • van der Biezen, E.A., Freddie, C.T., Kahn, K., Parker, J.E. Jones, J.D.G. (2002) Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR genes and confers downy mildew resistance through multiple signalling components. Plant J. 29, 439 51.
    • (2002) Plant J. , vol.29 , pp. 439-51
    • Van Der Biezen, E.A.1    Freddie, C.T.2    Kahn, K.3    Parker, J.E.4    Jones, J.D.G.5
  • 7
    • 0024368268 scopus 로고
    • Secretion of heterologous proteins directed by the yeast alpha-factor leader
    • Brake, A.J. (1989) Secretion of heterologous proteins directed by the yeast alpha-factor leader. Biotechnology, 13, 269 80.
    • (1989) Biotechnology , vol.13 , pp. 269-80
    • Brake, A.J.1
  • 9
    • 33645729843 scopus 로고    scopus 로고
    • Haustorially expressed secreted proteins from flax rust are highly enriched for avirulence elicitors
    • Catanzariti, A.M., Dodds, P.N., Lawrence, G.J., Ayliffe, M.A. Ellis, J.G. (2006) Haustorially expressed secreted proteins from flax rust are highly enriched for avirulence elicitors. Plant Cell, 18, 243 56.
    • (2006) Plant Cell , vol.18 , pp. 243-56
    • Catanzariti, A.M.1    Dodds, P.N.2    Lawrence, G.J.3    Ayliffe, M.A.4    Ellis, J.G.5
  • 10
    • 0029953324 scopus 로고    scopus 로고
    • Interactions of imidazole and proteins with immobilized Cu(II) ions: Effects of structure, salt concentration, and pH in affinity and binding capacity
    • Chen, W.Y., Wu, C.F. Liu, C.C. (1996) Interactions of imidazole and proteins with immobilized Cu(II) ions: effects of structure, salt concentration, and pH in affinity and binding capacity. J. Colloid Interface Sci. 180, 135 43.
    • (1996) J. Colloid Interface Sci. , vol.180 , pp. 135-43
    • Chen, W.Y.1    Wu, C.F.2    Liu, C.C.3
  • 11
    • 0034687842 scopus 로고    scopus 로고
    • Structure-function analysis of the tobacco mosaic virus resistance gene N
    • Dinesh-Kumar, S.P., Tham, W.H. Baker, B.J. (2000) Structure-function analysis of the tobacco mosaic virus resistance gene N. Proc. Natl Acad. Sci. USA, 97, 14789 94.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14789-94
    • Dinesh-Kumar, S.P.1    Tham, W.H.2    Baker, B.J.3
  • 12
    • 0035108614 scopus 로고    scopus 로고
    • Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax
    • Dodds, P.N., Lawrence, G.J. Ellis, J.G. (2001) Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax. Plant Cell, 13, 163 78.
    • (2001) Plant Cell , vol.13 , pp. 163-78
    • Dodds, P.N.1    Lawrence, G.J.2    Ellis, J.G.3
  • 13
    • 1542542334 scopus 로고    scopus 로고
    • The Melampsora lini AvrL567 avirulence genes are expressed in haustoria and their products are recognized inside plant cells
    • Dodds, P.N., Lawrence, G.J., Catanzariti, A.M., Ayliffe, M.A. Ellis, J.G. (2004) The Melampsora lini AvrL567 avirulence genes are expressed in haustoria and their products are recognized inside plant cells. Plant Cell, 16, 755 68.
    • (2004) Plant Cell , vol.16 , pp. 755-68
    • Dodds, P.N.1    Lawrence, G.J.2    Catanzariti, A.M.3    Ayliffe, M.A.4    Ellis, J.G.5
  • 14
    • 33745015480 scopus 로고    scopus 로고
    • Direct protein interaction underlies gene-for-gene specificity and coevolution of the flax resistance genes and flax rust avirulence genes
    • Dodds, P.N., Lawrence, G.J., Catanzariti, A.M., Teh, T., Wang, C.I.A., Ayliffe, M.A., Kobe, B. Ellis, J.G. (2006) Direct protein interaction underlies gene-for-gene specificity and coevolution of the flax resistance genes and flax rust avirulence genes. Proc. Natl Acad. Sci. USA, 103, 8888 93.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8888-93
    • Dodds, P.N.1    Lawrence, G.J.2    Catanzariti, A.M.3    Teh, T.4    Wang, C.I.A.5    Ayliffe, M.A.6    Kobe, B.7    Ellis, J.G.8
  • 16
    • 0033946441 scopus 로고    scopus 로고
    • Structure, function and evolution of plant disease resistance genes
    • Ellis, J., Dodds, P. Pryor, T. (2000) Structure, function and evolution of plant disease resistance genes. Curr. Opin. Plant Biol. 3, 278 84.
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 278-84
    • Ellis, J.1    Dodds, P.2    Pryor, T.3
  • 17
    • 77957077437 scopus 로고
    • The complementary genic systems in flax and flax rust
    • Flor, H.H. (1956) The complementary genic systems in flax and flax rust. Adv. Genet. 8, 29 54.
    • (1956) Adv. Genet. , vol.8 , pp. 29-54
    • Flor, H.H.1
  • 18
    • 0024425494 scopus 로고
    • Intracellular targeting and structural conservation of a prohormone-processing endoprotease
    • Fuller, R.S., Brake, A.J. Thorner, J. (1989) Intracellular targeting and structural conservation of a prohormone-processing endoprotease. Science, 246, 482 6.
    • (1989) Science , vol.246 , pp. 482-6
    • Fuller, R.S.1    Brake, A.J.2    Thorner, J.3
  • 19
    • 0032190378 scopus 로고    scopus 로고
    • Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography- microspray and nanospray mass spectrometry
    • Gatlin, C.L., Kleemann, G.R., Hays, L.G., Link, A.J. Yates, J.R. (1998) Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspray and nanospray mass spectrometry. Anal. Biochem. 263, 93 101.
    • (1998) Anal. Biochem. , vol.263 , pp. 93-101
    • Gatlin, C.L.1    Kleemann, G.R.2    Hays, L.G.3    Link, A.J.4    Yates, J.R.5
  • 20
    • 0001440524 scopus 로고
    • Present status of genetics of rust resistance in flax
    • Islam, M.R. Shepherd, K.W. (1991) Present status of genetics of rust resistance in flax. Euphytica, 55, 255 67.
    • (1991) Euphytica , vol.55 , pp. 255-67
    • Islam, M.R.1    Shepherd, K.W.2
  • 21
    • 0034254266 scopus 로고    scopus 로고
    • Direct interaction of resistance gene and avirulence gene products confers rice blast resistance
    • Jia, Y., McAdams, S.A., Bryan, G.T., Hershey, H.P. Valent, B. (2000) Direct interaction of resistance gene and avirulence gene products confers rice blast resistance. EMBO J. 19, 4004 14.
    • (2000) EMBO J. , vol.19 , pp. 4004-14
    • Jia, Y.1    McAdams, S.A.2    Bryan, G.T.3    Hershey, H.P.4    Valent, B.5
  • 22
    • 13844321118 scopus 로고    scopus 로고
    • Receptor-like proteins involved in plant disease resistance
    • Kruijt, M., De Kock, M.J.D. De Wit, P. (2005) Receptor-like proteins involved in plant disease resistance. Mol. Plant Pathol. 6, 85 97.
    • (2005) Mol. Plant Pathol. , vol.6 , pp. 85-97
    • Kruijt, M.1    De Kock, M.J.D.2    De Wit, P.3
  • 23
    • 0001919676 scopus 로고
    • Tagging rust resistance genes in flax
    • In. Iyama, S. Takeda, G. eds). Tsukuba, Japan: Organising Committee of the Sixth International Congress SABRAO, pp.
    • Lawrence, G.J., Ellis, J.G., Finnegan, E.J., Dennis, E.S. Peacock, W.J. (1989) Tagging rust resistance genes in flax. In Breeding Research: the Key To the Survival of the Earth (Iyama, S. Takeda, G. eds). Tsukuba, Japan : Organising Committee of the Sixth International Congress SABRAO, pp. 535 8.
    • (1989) Breeding Research: The Key to the Survival of the Earth , pp. 535-8
    • Lawrence, G.J.1    Ellis, J.G.2    Finnegan, E.J.3    Dennis, E.S.4    Peacock, W.J.5
  • 24
    • 0034045670 scopus 로고    scopus 로고
    • A resistance gene product of the nucleotide binding site - Leucine rich repeats class can form a complex with bacterial avirulence proteins in vivo
    • Leister, R.T. Katagiri, F. (2000) A resistance gene product of the nucleotide binding site - leucine rich repeats class can form a complex with bacterial avirulence proteins in vivo. Plant J. 22, 345 54.
    • (2000) Plant J. , vol.22 , pp. 345-54
    • Leister, R.T.1    Katagiri, F.2
  • 25
    • 0032212087 scopus 로고    scopus 로고
    • A flax transposon identified in two spontaneous mutant alleles of the L6 rust resistance gene
    • Luck, J.E., Lawrence, G.J., Finnegan, E.J., Jones, D.A. Ellis, J.G. (1998) A flax transposon identified in two spontaneous mutant alleles of the L6 rust resistance gene. Plant J. 16, 365 9.
    • (1998) Plant J. , vol.16 , pp. 365-9
    • Luck, J.E.1    Lawrence, G.J.2    Finnegan, E.J.3    Jones, D.A.4    Ellis, J.G.5
  • 26
    • 0033180530 scopus 로고    scopus 로고
    • Functional analysis of plant disease resistance genes and their downstream effectors
    • Martin, G.B. (1999) Functional analysis of plant disease resistance genes and their downstream effectors. Curr. Opin. Plant Biol. 2, 273 9.
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 273-9
    • Martin, G.B.1
  • 27
    • 33745455354 scopus 로고    scopus 로고
    • Elicitor-mediated oligomerization of the tobacco N disease resistance protein
    • Mestre, P. Baulcombe, D.C. (2006) Elicitor-mediated oligomerization of the tobacco N disease resistance protein. Plant Cell, 18, 491 501.
    • (2006) Plant Cell , vol.18 , pp. 491-501
    • Mestre, P.1    Baulcombe, D.C.2
  • 28
    • 0033231602 scopus 로고    scopus 로고
    • Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily
    • Meyers, B.C., Dickerman, A.W., Michelmore, R.W., Sivaramakrishnan, S., Sobral, B.W. Young, N.D. (1999) Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily. Plant J. 20, 317 32.
    • (1999) Plant J. , vol.20 , pp. 317-32
    • Meyers, B.C.1    Dickerman, A.W.2    Michelmore, R.W.3    Sivaramakrishnan, S.4    Sobral, B.W.5    Young, N.D.6
  • 30
    • 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, D.C. (2002) Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death. EMBO J. 21, 4511 9.
    • (2002) EMBO J. , vol.21 , pp. 4511-9
    • Moffett, P.1    Farnham, G.2    Peart, J.3    Baulcombe, D.C.4
  • 31
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S. vonHeijne, G. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1 6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Vonheijne, G.4
  • 32
    • 0035504591 scopus 로고    scopus 로고
    • Interactions of proteins with immobilized metal ions - Role of ionic strength and pH
    • Sharma, S. Agarwal, G.P. (2001) Interactions of proteins with immobilized metal ions - Role of ionic strength and pH. J. Colloid Interface Sci. 243, 61 72.
    • (2001) J. Colloid Interface Sci. , vol.243 , pp. 61-72
    • Sharma, S.1    Agarwal, G.P.2
  • 33
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. Woody, R.W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252 60.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-60
    • Sreerama, N.1    Woody, R.W.2
  • 34
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama, N. Woody, R.W. (2004) Computation and analysis of protein circular dichroism spectra. Method Enzymol. 383, 318 51.
    • (2004) Method Enzymol. , vol.383 , pp. 318-51
    • Sreerama, N.1    Woody, R.W.2
  • 36
    • 0031608474 scopus 로고    scopus 로고
    • High cell-density fermentation
    • In. Higgins, D.R. Cregg, J.M. eds). Totowa, New Jersey: Humana Press, pp.
    • Stratton, J., Chiruvolu, V. Meagher, M. (1998) High cell-density fermentation. In Pichia Protocols (Higgins, D.R. Cregg, J.M. eds). Totowa, New Jersey : Humana Press, pp. 107 20.
    • (1998) Pichia Protocols , pp. 107-20
    • Stratton, J.1    Chiruvolu, V.2    Meagher, M.3
  • 39
    • 0034489715 scopus 로고    scopus 로고
    • Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2
    • Tao, Y., Yuan, F.H., Leister, R.T., Ausubel, F.M. Katagiri, F. (2000) Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2. Plant Cell, 12, 2541 54.
    • (2000) Plant Cell , vol.12 , pp. 2541-54
    • Tao, Y.1    Yuan, F.H.2    Leister, R.T.3    Ausubel, F.M.4    Katagiri, F.5
  • 40
    • 33745184517 scopus 로고    scopus 로고
    • Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants
    • Ueda, H., Yamaguchi, Y. Sano, H. (2006) Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants. Plant Mol. Biol. 61, 31 45.
    • (2006) Plant Mol. Biol. , vol.61 , pp. 31-45
    • Ueda, H.1    Yamaguchi, Y.2    Sano, H.3
  • 41
    • 0036272947 scopus 로고    scopus 로고
    • A dual role for microbial pathogen-derived effector proteins in plant disease and resistance
    • van't Slot, K.A.E. Knogge, W. (2002) A dual role for microbial pathogen-derived effector proteins in plant disease and resistance. Crit. Rev. Plant. Sci. 21, 229 71.
    • (2002) Crit. Rev. Plant. Sci. , vol.21 , pp. 229-71
    • Van'T Slot, K.A.E.1    Knogge, W.2
  • 42
    • 0032170811 scopus 로고    scopus 로고
    • A mutation within the leucine-rich repeat domain of the Arabidopsis disease resistance gene RPS5 partially suppresses multiple bacterial and downy mildew resistance genes
    • Warren, R.F., Henk, A., Mowery, P., Holub, E. Innes, R.W. (1998) A mutation within the leucine-rich repeat domain of the Arabidopsis disease resistance gene RPS5 partially suppresses multiple bacterial and downy mildew resistance genes. Plant Cell, 10, 1439 52.
    • (1998) Plant Cell , vol.10 , pp. 1439-52
    • Warren, R.F.1    Henk, A.2    Mowery, P.3    Holub, E.4    Innes, R.W.5
  • 43
    • 0000680432 scopus 로고
    • Studies of chemically reacting systems on sephadex 1. Chromatographic demonstration of Gilbert theory
    • Winzor, D.J. Scheraga, H.A. (1963) Studies of chemically reacting systems on sephadex 1. Chromatographic demonstration of Gilbert theory. Biochemistry, 2, 1263.
    • (1963) Biochemistry , vol.2 , pp. 1263
    • Winzor, D.J.1    Scheraga, H.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.