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Volumn 17, Issue 7, 2008, Pages 1109-1119

Folding kinetics and thermodynamics of Pseudomonas syringae effector protein AvrPto provide insight into translocation via the type III secretion system

Author keywords

AvrPto; Low stability; pH dependent stability; Pseudomonas syringae; Slow conformational exchange; Type III secretion system

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEIN AVRPTO;

EID: 46449093638     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.034223.107     Document Type: Article
Times cited : (4)

References (74)
  • 2
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda, Y. and Galan, J.E. 2005. Chaperone release and unfolding of substrates in type III secretion. Nature 437: 911-915.
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 3
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson, D.M. and Schneewind, O. 1997. A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 278: 1140-1143.
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 4
    • 33645954277 scopus 로고    scopus 로고
    • Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR
    • Bezsonova, I., Korzhnev, D.M., Prosser, R.S., Forman-Kay, J.D., and Kay, L.E. 2006. Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR. Biochemistry 45: 4711-4719.
    • (2006) Biochemistry , vol.45 , pp. 4711-4719
    • Bezsonova, I.1    Korzhnev, D.M.2    Prosser, R.S.3    Forman-Kay, J.D.4    Kay, L.E.5
  • 6
    • 0034255015 scopus 로고    scopus 로고
    • AvrPto-dependent Pto-interacting proteins and AvrPto-inteacting proteins in tomato
    • Bogdanove, A.J. and Martin, G.B. 2000. AvrPto-dependent Pto-interacting proteins and AvrPto-inteacting proteins in tomato. Proc. Natl. Acad. Sci. 97: 8836-8840.
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 8836-8840
    • Bogdanove, A.J.1    Martin, G.B.2
  • 7
    • 0035114376 scopus 로고    scopus 로고
    • Immunocytochemical localization of HrpA and HrpZ supports a role for the Hrp Ilus in the transfer of effector proteins from Pseudomonas syringae pv. tomato across the host plant cell wall
    • Brown, I.R., Mansfield, J.W., Taira, S., Roine, E., and Romantschuk, M. 2001. Immunocytochemical localization of HrpA and HrpZ supports a role for the Hrp Ilus in the transfer of effector proteins from Pseudomonas syringae pv. tomato across the host plant cell wall. Mol. Plant-Microbe Interact. 14: 394-404.
    • (2001) Mol. Plant-Microbe Interact , vol.14 , pp. 394-404
    • Brown, I.R.1    Mansfield, J.W.2    Taira, S.3    Roine, E.4    Romantschuk, M.5
  • 9
    • 0034001870 scopus 로고    scopus 로고
    • AvrPto enhances growth and necrosis caused by Pseudomonas syringae pv. tomato in tomato lines lacking either Pto or Prf
    • Chang, J.H., Rathjen, J.P., Bernal, A.J., Staskawicz, B.J., and Michelmore, R.W. 2000. AvrPto enhances growth and necrosis caused by Pseudomonas syringae pv. tomato in tomato lines lacking either Pto or Prf. Mol. Plant-Microbe Interact. 13: 568-571.
    • (2000) Mol. Plant-Microbe Interact , vol.13 , pp. 568-571
    • Chang, J.H.1    Rathjen, J.P.2    Bernal, A.J.3    Staskawicz, B.J.4    Michelmore, R.W.5
  • 10
    • 0033618257 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells
    • Cheng, L.W. and Schneewind, O. 1999. Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells. J. Biol. Chem. 274: 22102-22108.
    • (1999) J. Biol. Chem , vol.274 , pp. 22102-22108
    • Cheng, L.W.1    Schneewind, O.2
  • 11
    • 0038608020 scopus 로고    scopus 로고
    • Helical structure of the needle of the type III secretion system of Shigella flexneri
    • Cordes, F.S., Komoriya, K., Larquet, E., Yang, S., Egelman, E.H., Blocker, A., and Lea, S.M. 2003. Helical structure of the needle of the type III secretion system of Shigella flexneri. J. Biol. Chem. 278: 17103-17107.
    • (2003) J. Biol. Chem , vol.278 , pp. 17103-17107
    • Cordes, F.S.1    Komoriya, K.2    Larquet, E.3    Yang, S.4    Egelman, E.H.5    Blocker, A.6    Lea, S.M.7
  • 12
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 13
    • 0027941071 scopus 로고
    • Molecular and functional characterization of the Salmonella typhimurium invasion genes invB and invC: Homology of InvC to the F0F1 ATPase family of proteins
    • Eichelberg, K., Ginocchio, C.C., and Galan, J.E. 1994. Molecular and functional characterization of the Salmonella typhimurium invasion genes invB and invC: Homology of InvC to the F0F1 ATPase family of proteins. J. Bacteriol. 176: 4501-4510.
    • (1994) J. Bacteriol , vol.176 , pp. 4501-4510
    • Eichelberg, K.1    Ginocchio, C.C.2    Galan, J.E.3
  • 14
    • 0014939798 scopus 로고
    • Bacterial flagella: Polarity of elongation
    • Emerson, S.U., Tokuyasu, K., and Simon, M.I. 1970. Bacterial flagella: Polarity of elongation. Science 169: 190-192.
    • (1970) Science , vol.169 , pp. 190-192
    • Emerson, S.U.1    Tokuyasu, K.2    Simon, M.I.3
  • 15
  • 19
    • 0029070827 scopus 로고
    • The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci
    • Frithz-Lindsten, E., Rosqvist, R., Johansson, L., and Forsberg, A. 1995. The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci. Mol. Microbiol. 16: 635-647.
    • (1995) Mol. Microbiol , vol.16 , pp. 635-647
    • Frithz-Lindsten, E.1    Rosqvist, R.2    Johansson, L.3    Forsberg, A.4
  • 20
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • Galan, J.E. and Collmer, A. 1999. Type III secretion machines: Bacterial devices for protein delivery into host cells. Science 284: 1322-1328.
    • (1999) Science , vol.284 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 22
    • 10344249890 scopus 로고    scopus 로고
    • Process of protein transport by the type III secretion system
    • Ghosh, P. 2004. Process of protein transport by the type III secretion system. Microbiol. Mol. Biol. Rev. 68: 771-795.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 771-795
    • Ghosh, P.1
  • 23
    • 0027182114 scopus 로고
    • Helicases-amino-acid-sequence comparisons and structure-function-relationships
    • Gorbalenya, A.E. and Koonin, E.V. 1993. Helicases-amino-acid-sequence comparisons and structure-function-relationships. Curr. Opin. Struct. Biol. 3: 419-429.
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 24
    • 0038152973 scopus 로고    scopus 로고
    • A Pseudomonas syringae type III effector suppresses cell wall-based extracellular defense in susceptible Arabidopsis plants
    • Hauck, P., Thilmony, R., and He, S.Y. 2003. A Pseudomonas syringae type III effector suppresses cell wall-based extracellular defense in susceptible Arabidopsis plants. Proc. Natl. Acad. Sci. 100: 8577-8582.
    • (2003) Proc. Natl. Acad. Sci , vol.100 , pp. 8577-8582
    • Hauck, P.1    Thilmony, R.2    He, S.Y.3
  • 25
    • 35648986559 scopus 로고    scopus 로고
    • Thermodynamic dissection of the Ezrin FERM/CERMAD interface
    • Jayaraman, B. and Nicholson, L.K. 2007. Thermodynamic dissection of the Ezrin FERM/CERMAD interface. Biochemistry 46: 12174-12189.
    • (2007) Biochemistry , vol.46 , pp. 12174-12189
    • Jayaraman, B.1    Nicholson, L.K.2
  • 28
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston, J.A., Baker, T.A., Fernandez, J.M., and Sauer, R.T. 2003. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114: 511-520.
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-55.
    • (1996) J. Mol. Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 30
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M., and Matouschek, A. 2001. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7: 627-637.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 31
    • 0036283447 scopus 로고    scopus 로고
    • Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion
    • Lee, V.T. and Schneewind, O. 2002. Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion. J. Bacteriol. 184: 3740-3745.
    • (2002) J. Bacteriol , vol.184 , pp. 3740-3745
    • Lee, V.T.1    Schneewind, O.2
  • 32
    • 0001114489 scopus 로고
    • Relaxation times in systems with chemical exchange: Some exact solutions
    • Leigh, J.S. 1971. Relaxation times in systems with chemical exchange: Some exact solutions. J. Magn. Reson. 4: 308-311.
    • (1971) J. Magn. Reson , vol.4 , pp. 308-311
    • Leigh, J.S.1
  • 33
    • 0000873069 scopus 로고
    • A method for the solution of certain problems in least squares
    • Levenberg, K. 1944. A method for the solution of certain problems in least squares. Q. Appl. Math. 2: 164-168.
    • (1944) Q. Appl. Math , vol.2 , pp. 164-168
    • Levenberg, K.1
  • 34
    • 0037090775 scopus 로고    scopus 로고
    • The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ
    • Li, C.M., Brown, I., Mansfield, J., Stevens, C., Boureau, T., Romantschuk, M., and Taira, S. 2002. The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ. EMBO J. 21: 1909-1915.
    • (2002) EMBO J , vol.21 , pp. 1909-1915
    • Li, C.M.1    Brown, I.2    Mansfield, J.3    Stevens, C.4    Boureau, T.5    Romantschuk, M.6    Taira, S.7
  • 35
    • 33845553743 scopus 로고
    • Model-free analysis to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari, G. and Szabo, A. 1982. Model-free analysis to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104: 4559-4570.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 38
    • 0000169232 scopus 로고
    • An algorithm of least-squares estimation of nonlinear parameters
    • Marquardt, D. 1963. An algorithm of least-squares estimation of nonlinear parameters. SIAM J. Appl. Math. 11: 431-441.
    • (1963) SIAM J. Appl. Math , vol.11 , pp. 431-441
    • Marquardt, D.1
  • 39
    • 0037308999 scopus 로고    scopus 로고
    • Protein unfolding - an important process in vivo?
    • Matouschek, A. 2003. Protein unfolding - an important process in vivo? Curr. Opin. Struct. Biol. 13: 98-109.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 98-109
    • Matouschek, A.1
  • 40
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • McConnell, H.M. 1958. Reaction rates by nuclear magnetic resonance. J. Chem. Phys. 28: 430-431.
    • (1958) J. Chem. Phys , vol.28 , pp. 430-431
    • McConnell, H.M.1
  • 41
    • 0037317217 scopus 로고    scopus 로고
    • Effect of intracellular pH on rotational speed of bacterial flagellar motors
    • Minamino, T., Imae, Y., Oosawa, F., Kobayashi, Y., and Oosawa, K. 2003. Effect of intracellular pH on rotational speed of bacterial flagellar motors. J. Bacteriol. 185: 1190-1194.
    • (2003) J. Bacteriol , vol.185 , pp. 1190-1194
    • Minamino, T.1    Imae, Y.2    Oosawa, F.3    Kobayashi, Y.4    Oosawa, K.5
  • 42
    • 33845182844 scopus 로고
    • 2D chemical-exchange NMR-spectroscopy by proton-detected heteronuclear correlation
    • Montelione, G.T. and Wagner, G. 1989. 2D chemical-exchange NMR-spectroscopy by proton-detected heteronuclear correlation. J. Am. Chem. Soc. 111: 3096-3098.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 3096-3098
    • Montelione, G.T.1    Wagner, G.2
  • 43
  • 44
    • 34548849769 scopus 로고    scopus 로고
    • Solvation and desolvation dynamics in apomyoglobin folding monitored by time-resolved infrared spectroscopy
    • Nishiguchi, S., Goto, Y., and Takahashi, S. 2007. Solvation and desolvation dynamics in apomyoglobin folding monitored by time-resolved infrared spectroscopy. J. Mol. Biol. 373: 491-502.
    • (2007) J. Mol. Biol , vol.373 , pp. 491-502
    • Nishiguchi, S.1    Goto, Y.2    Takahashi, S.3
  • 45
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer, A.G.I. 2001. NMR probes of molecular dynamics: Overview and comparison with other techniques. Annu. Rev. Biophys. Biomol. Struct. 30: 129-155.
    • (2001) Annu. Rev. Biophys. Biomol. Struct , vol.30 , pp. 129-155
    • Palmer, A.G.I.1
  • 47
    • 0036873003 scopus 로고    scopus 로고
    • Factors determining the reliable description of global tumbling parameters in solution NMR
    • Pawley, N.H., Gans, J.D., and Nicholson, L.K. 2002. Factors determining the reliable description of global tumbling parameters in solution NMR. J. Biomol. NMR 24: 215-229.
    • (2002) J. Biomol. NMR , vol.24 , pp. 215-229
    • Pawley, N.H.1    Gans, J.D.2    Nicholson, L.K.3
  • 48
    • 0242406897 scopus 로고    scopus 로고
    • Molecular basis of Pto-mediated resistance to bacterial speck disease in tomato
    • Pedley, K.F. and Martin, G.B. 2003. Molecular basis of Pto-mediated resistance to bacterial speck disease in tomato. Annu. Rev. Phytopathol. 41: 215-243.
    • (2003) Annu. Rev. Phytopathol , vol.41 , pp. 215-243
    • Pedley, K.F.1    Martin, G.B.2
  • 49
    • 34447509491 scopus 로고    scopus 로고
    • On the application of CZE to the study of protein denaturation
    • Piaggio, M.V., Peirotti, M.B., and Deiber, J.A. 2007. On the application of CZE to the study of protein denaturation. Electrophoresis 28: 2223-2234.
    • (2007) Electrophoresis , vol.28 , pp. 2223-2234
    • Piaggio, M.V.1    Peirotti, M.B.2    Deiber, J.A.3
  • 51
    • 0029377306 scopus 로고
    • The HrpZ proteins of Pseudomonas syringae pvs. Syringae, glycinea, and tomato are encoded by an operon containing Yersinia ysc homologs and elicit the hypersensitive response in tomato but not soybean
    • Preston, G., Huang, H.C., He, S.Y., and Collmer, A. 1995. The HrpZ proteins of Pseudomonas syringae pvs. Syringae, glycinea, and tomato are encoded by an operon containing Yersinia ysc homologs and elicit the hypersensitive response in tomato but not soybean. Mol Plant-Microbe Interact. 8: 717-732.
    • (1995) Mol Plant-Microbe Interact , vol.8 , pp. 717-732
    • Preston, G.1    Huang, H.C.2    He, S.Y.3    Collmer, A.4
  • 52
    • 0026642188 scopus 로고
    • Plant and environmental sensory signals control the expression of hrp genes in Pseudomonas syringae pv. phaseolicola
    • Rahme, L.G., Mindrinos, M.N., and Panopoulos, N.J. 1992. Plant and environmental sensory signals control the expression of hrp genes in Pseudomonas syringae pv. phaseolicola. J. Bacteriol. 174: 3499-3507.
    • (1992) J. Bacteriol , vol.174 , pp. 3499-3507
    • Rahme, L.G.1    Mindrinos, M.N.2    Panopoulos, N.J.3
  • 53
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., Magnusson, K.E., and Wolf-Wantz, H. 1994. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13: 964-972.
    • (1994) EMBO J , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf-Wantz, H.3
  • 55
    • 0028541223 scopus 로고
    • A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization
    • Schurr, J.M., Babcock, H.P., and Fujimoto, B.S. 1994. A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. J. Magn. Reson. B. 105: 211-224.
    • (1994) J. Magn. Reson. B , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.S.3
  • 57
    • 0034029316 scopus 로고    scopus 로고
    • A cluster of mutations disrupt the antivirulence but not the virulence function of AvrPto
    • Shan, L., He, P., Zhou, J.M., and Tang, X. 2000. A cluster of mutations disrupt the antivirulence but not the virulence function of AvrPto. Mol. Plant-Microbe Interact. 13: 592-598.
    • (2000) Mol. Plant-Microbe Interact , vol.13 , pp. 592-598
    • Shan, L.1    He, P.2    Zhou, J.M.3    Tang, X.4
  • 58
    • 0037058992 scopus 로고    scopus 로고
    • Probing the folding free energy landscape of the Src-SH3 protein domain
    • Shea, J.E., Onuchic, J.N., and Brooks III, C.L. 2002. Probing the folding free energy landscape of the Src-SH3 protein domain. Proc. Natl. Acad. Sci. 99: 16064-16068.
    • (2002) Proc. Natl. Acad. Sci , vol.99 , pp. 16064-16068
    • Shea, J.E.1    Onuchic, J.N.2    Brooks III, C.L.3
  • 59
    • 26444526690 scopus 로고    scopus 로고
    • Rejection of impassable substrates by Yerinia type III secretion machines
    • Sorg, J.A., Miller, N.C., Marketon, M.M., and Schneewind, O. 2005. Rejection of impassable substrates by Yerinia type III secretion machines. J. Bacteriol. 187: 7090-7102.
    • (2005) J. Bacteriol , vol.187 , pp. 7090-7102
    • Sorg, J.A.1    Miller, N.C.2    Marketon, M.M.3    Schneewind, O.4
  • 60
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory, M.P. and Cornelis, G.R. 1994. Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol. Microbiol. 14: 583-594.
    • (1994) Mol. Microbiol , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 61
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C.E. and Galan, J.E. 2001. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414: 77-81.
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 62
    • 0034254475 scopus 로고    scopus 로고
    • Supramolecular structure of the Shigella type III secretion machinery: The needle part is changeable in length and essential for delivery of effectors
    • Tamano, K., Aizawa, S., Katayama, E., Nonaka, T., Imajoh-Ohmi, S., Kuwae, A., Nagai, S., and Sasakawa, C. 2000. Supramolecular structure of the Shigella type III secretion machinery: The needle part is changeable in length and essential for delivery of effectors. EMBO J. 19: 3876-3887.
    • (2000) EMBO J , vol.19 , pp. 3876-3887
    • Tamano, K.1    Aizawa, S.2    Katayama, E.3    Nonaka, T.4    Imajoh-Ohmi, S.5    Kuwae, A.6    Nagai, S.7    Sasakawa, C.8
  • 63
    • 0032750816 scopus 로고    scopus 로고
    • Overexpression of Pto activates defense responses and confers broad resistance
    • Tang, X., Xie, M., Kim, Y.J., Zhou, J., Klessing, D.F., and Martin, G.B. 1999. Overexpression of Pto activates defense responses and confers broad resistance. Plant Cell 11: 15-29.
    • (1999) Plant Cell , vol.11 , pp. 15-29
    • Tang, X.1    Xie, M.2    Kim, Y.J.3    Zhou, J.4    Klessing, D.F.5    Martin, G.B.6
  • 64
    • 0032864453 scopus 로고    scopus 로고
    • The Avr (effector) proteins HrmA (HopPsyA) and AvrPto are secreted in culture from Pseudomonas syringae pathovars via the Hrp (type III) protein secretion system in a temperature- and pH-sensitive manner
    • van Dijk, K., Fouts, D.E., Rehm, A.H., Hill, A.R., Collmer, A., and Alfano, J.R. 1999. The Avr (effector) proteins HrmA (HopPsyA) and AvrPto are secreted in culture from Pseudomonas syringae pathovars via the Hrp (type III) protein secretion system in a temperature- and pH-sensitive manner. J. Bacteriol. 181: 4790-4797.
    • (1999) J. Bacteriol , vol.181 , pp. 4790-4797
    • van Dijk, K.1    Fouts, D.E.2    Rehm, A.H.3    Hill, A.R.4    Collmer, A.5    Alfano, J.R.6
  • 67
    • 3042692057 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB
    • Wilharm, G., Lehmann, V., Krauss, K., Lehnert, B., Richter, S., Ruckdeschel, K., Heesemann, J., and Trulzsch, K. 2004. Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB. Infect. Immun. 72: 4004-4009.
    • (2004) Infect. Immun , vol.72 , pp. 4004-4009
    • Wilharm, G.1    Lehmann, V.2    Krauss, K.3    Lehnert, B.4    Richter, S.5    Ruckdeschel, K.6    Heesemann, J.7    Trulzsch, K.8
  • 68
    • 33644625296 scopus 로고
    • Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion
    • Woessner, D.E. 1962. Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion. J. Chem. Phys. 37: 647-654.
    • (1962) J. Chem. Phys , vol.37 , pp. 647-654
    • Woessner, D.E.1
  • 69
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S., Allaoui, A., Wattiau, P., and Cornelis, G.R. 1994. YscN, the putative energizer of the Yersinia Yop secretion machinery. J. Bacteriol. 176: 1561-1569.
    • (1994) J. Bacteriol , vol.176 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.R.4
  • 70
    • 3142534455 scopus 로고    scopus 로고
    • The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis
    • Wulf, J., Pascuzzi, P.E., Fahmy, A., Martin, G.B., and Nicholson, L.K. 2004. The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis. Structure 12: 1257-1268.
    • (2004) Structure , vol.12 , pp. 1257-1268
    • Wulf, J.1    Pascuzzi, P.E.2    Fahmy, A.3    Martin, G.B.4    Nicholson, L.K.5
  • 71
    • 0036170459 scopus 로고    scopus 로고
    • LcrQ and SycH function together a the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion
    • Wulff-Strobel, C.R., Williams, A.W., and Straley, S.C. 2002. LcrQ and SycH function together a the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion. Mol. Microbiol. 43: 411-423.
    • (2002) Mol. Microbiol , vol.43 , pp. 411-423
    • Wulff-Strobel, C.R.1    Williams, A.W.2    Straley, S.C.3
  • 72
    • 0026577851 scopus 로고
    • Organization and environmental regulation of the Pseudomonas syringae pv. syringae 61 hrp cluster
    • Xiao, Y., Lu, Y., Heu, S., and Hutcheson, S.W. 1992. Organization and environmental regulation of the Pseudomonas syringae pv. syringae 61 hrp cluster. J. Bacteriol. 174: 1734-1741.
    • (1992) J. Bacteriol , vol.174 , pp. 1734-1741
    • Xiao, Y.1    Lu, Y.2    Heu, S.3    Hutcheson, S.W.4
  • 73
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura, K., Maki-Yonekura, S., and Namba, K. 2003. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424: 643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 74
    • 0027058169 scopus 로고
    • Expression, purification, and physiochemical characterization of a recombinant Yersinia protein tyrosine phosphatase
    • Zhang, Z.Y., Clemens, J.C., Schubert, H.L., Stuckey, J.A., Fischer, M.W., Hume, D.M., Saper, M.A., and Dixon, J.E. 1992. Expression, purification, and physiochemical characterization of a recombinant Yersinia protein tyrosine phosphatase. J. Biol. Chem. 267: 23759-23766.
    • (1992) J. Biol. Chem , vol.267 , pp. 23759-23766
    • Zhang, Z.Y.1    Clemens, J.C.2    Schubert, H.L.3    Stuckey, J.A.4    Fischer, M.W.5    Hume, D.M.6    Saper, M.A.7    Dixon, J.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.