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Volumn 411, Issue 3, 2008, Pages 485-493

The guanine-nucleotide-exchange factor BopE from Burkholderia pseudomallei adopts a compact version of the Salmonella SopE/SopE2 fold and undergoes a closed-to-open conformational change upon interaction with Cdc42

Author keywords

Bacterial pathogen; Guanine nucleotide exchange factor; Protein structure; Protein protein interaction; Rho GTPase; Type III secretion

Indexed keywords

CATALYST ACTIVITY; CONFORMATIONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDES; PATHOGENS;

EID: 42449139551     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071546     Document Type: Article
Times cited : (20)

References (52)
  • 1
    • 0036212489 scopus 로고    scopus 로고
    • Dance, D. A. B. (2002) Melioidosis. Curr. Opin. Infect. Dis. 15, 127-132
    • Dance, D. A. B. (2002) Melioidosis. Curr. Opin. Infect. Dis. 15, 127-132
  • 2
    • 0038324480 scopus 로고    scopus 로고
    • Melioidosis
    • White, N. J. (2003) Melioidosis. Lancet 361, 1715-1722
    • (2003) Lancet , vol.361 , pp. 1715-1722
    • White, N.J.1
  • 3
    • 33748343781 scopus 로고    scopus 로고
    • Peacock, S. J. (2006) Melioidosis. Curr. Opin. Infect. Dis. 19, 421-428
    • Peacock, S. J. (2006) Melioidosis. Curr. Opin. Infect. Dis. 19, 421-428
  • 4
    • 0033959534 scopus 로고    scopus 로고
    • Pathogenesis of and immunity to melioidosis
    • Brett, P. J. and Woods, D. E. (2000) Pathogenesis of and immunity to melioidosis. Acta Tropica 74, 201-210
    • (2000) Acta Tropica , vol.74 , pp. 201-210
    • Brett, P.J.1    Woods, D.E.2
  • 8
    • 0019835925 scopus 로고
    • Glanders: Medicine and veterinary medicine in common pursuit of a contagious disease
    • Wilkinson, L. (1981) Glanders: medicine and veterinary medicine in common pursuit of a contagious disease. Med. Hist. 25, 363-384
    • (1981) Med. Hist , vol.25 , pp. 363-384
    • Wilkinson, L.1
  • 9
  • 10
    • 33750353841 scopus 로고    scopus 로고
    • A live experimental vaccine against Burkholderia pseudomallei elicits CD4(+) T cell-mediated immunity, priming T cells specific for 2 type III secretion system proteins
    • Haque, A., Chu, K., Easton, A., Stevens, M. P., Galyov, E. E., Atkins, T., Titball, R. and Bancroft, G. J. (2006) A live experimental vaccine against Burkholderia pseudomallei elicits CD4(+) T cell-mediated immunity, priming T cells specific for 2 type III secretion system proteins. J. Infect. Dis. 194, 1241-1248
    • (2006) J. Infect. Dis , vol.194 , pp. 1241-1248
    • Haque, A.1    Chu, K.2    Easton, A.3    Stevens, M.P.4    Galyov, E.E.5    Atkins, T.6    Titball, R.7    Bancroft, G.J.8
  • 11
    • 2442639049 scopus 로고    scopus 로고
    • Exploitation of host cells by Burkholderia pseudomallei
    • Stevens, M. P. and Galyov, E. E. (2004) Exploitation of host cells by Burkholderia pseudomallei. Int. J. Med. Microbiol. 293, 549-555
    • (2004) Int. J. Med. Microbiol , vol.293 , pp. 549-555
    • Stevens, M.P.1    Galyov, E.E.2
  • 13
    • 0036242813 scopus 로고    scopus 로고
    • Distribution of type III secretion gene clusters in Burkholderia pseudomallei, B. thailandensis and B. mallei
    • Rainbow, L., Hart, C. A. and Winstanley, G. (2002) Distribution of type III secretion gene clusters in Burkholderia pseudomallei, B. thailandensis and B. mallei. J. Med. Microbiol. 51, 374-384
    • (2002) J. Med. Microbiol , vol.51 , pp. 374-384
    • Rainbow, L.1    Hart, C.A.2    Winstanley, G.3
  • 14
    • 0035217519 scopus 로고    scopus 로고
    • A second type III secretion system in Burkholderia pseudomallei: Who is the real culprit?
    • Attree, O. and Attree, I. (2001) A second type III secretion system in Burkholderia pseudomallei: who is the real culprit? Microbiology 147, 3197-3199
    • (2001) Microbiology , vol.147 , pp. 3197-3199
    • Attree, O.1    Attree, I.2
  • 15
    • 0036441427 scopus 로고    scopus 로고
    • An inv/mxi-spa-like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen
    • Stevens, M. P., Wood, M. W., Taylor, L. A., Monaghan, P., Hawes, P., Jones, P. W., Wallis, T. S. and Galyov, E. E. (2002) An inv/mxi-spa-like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen. Mol. Microbiol. 46, 649-659
    • (2002) Mol. Microbiol , vol.46 , pp. 649-659
    • Stevens, M.P.1    Wood, M.W.2    Taylor, L.A.3    Monaghan, P.4    Hawes, P.5    Jones, P.W.6    Wallis, T.S.7    Galyov, E.E.8
  • 17
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galàn, J. E. and Wolf-Watz, H. (2006) Protein delivery into eukaryotic cells by type III secretion machines. Nature 444, 567-573
    • (2006) Nature , vol.444 , pp. 567-573
    • Galàn, J.E.1    Wolf-Watz, H.2
  • 18
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornells, G. R. and Van Gijsegem, F. (2000) Assembly and function of type III secretory systems. Annu. Rev. Microbiol. 54, 735-774
    • (2000) Annu. Rev. Microbiol , vol.54 , pp. 735-774
    • Cornells, G.R.1    Van Gijsegem, F.2
  • 19
    • 15944409588 scopus 로고    scopus 로고
    • Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: A Darwinian perspective
    • Pallen, M. J., Beatson, S. A. and Bailey, C. M. (2005) Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perspective. FEMS Microbiol. Rev. 29, 201-229
    • (2005) FEMS Microbiol. Rev , vol.29 , pp. 201-229
    • Pallen, M.J.1    Beatson, S.A.2    Bailey, C.M.3
  • 20
    • 0041530031 scopus 로고    scopus 로고
    • A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity
    • Stevens, M. P., Friebel, A., Taylor, L. A., Wood, M. W., Brown, P. J., Hardt, W.-D. and Galyov, E. E. (2003) A Burkholderia pseudomallei type III secreted protein, BopE, facilitates bacterial invasion of epithelial cells and exhibits guanine nucleotide exchange factor activity. J. Bacteriol. 185, 4992-4996
    • (2003) J. Bacteriol , vol.185 , pp. 4992-4996
    • Stevens, M.P.1    Friebel, A.2    Taylor, L.A.3    Wood, M.W.4    Brown, P.J.5    Hardt, W.-D.6    Galyov, E.E.7
  • 21
    • 0029806327 scopus 로고    scopus 로고
    • SopE, a secreted protein of Salmonella dublin, is translocated into the target eukaryotic cell via a Sip-dependent mechanism and promotes bacterial entry
    • Wood, M. W., Rosqvist, R., Mullan, P. B., Edwards, M. H. and Galyov, E. E. (1996) SopE, a secreted protein of Salmonella dublin, is translocated into the target eukaryotic cell via a Sip-dependent mechanism and promotes bacterial entry. Mol. Microbiol. 22, 327-338
    • (1996) Mol. Microbiol , vol.22 , pp. 327-338
    • Wood, M.W.1    Rosqvist, R.2    Mullan, P.B.3    Edwards, M.H.4    Galyov, E.E.5
  • 22
    • 0032577563 scopus 로고    scopus 로고
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R. and Galàn, J. E. (1998) S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R. and Galàn, J. E. (1998) S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826
  • 23
    • 0034074961 scopus 로고    scopus 로고
    • Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells
    • Bakshi, C. S., Singh, V. P., Wood, M. W., Jones, P. W., Wallis, T. S. and Galyov, E. E. (2000) Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells. J. Bacteriol. 182, 2341-2344
    • (2000) J. Bacteriol , vol.182 , pp. 2341-2344
    • Bakshi, C.S.1    Singh, V.P.2    Wood, M.W.3    Jones, P.W.4    Wallis, T.S.5    Galyov, E.E.6
  • 24
    • 0033923731 scopus 로고    scopus 로고
    • Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell
    • Stender, S., Friebel, A., Linder, S., Rohde, M., Mirold, S. and Hardt, W. D. (2000) Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell. Mol. Microbiol. 36, 1206-1221
    • (2000) Mol. Microbiol , vol.36 , pp. 1206-1221
    • Stender, S.1    Friebel, A.2    Linder, S.3    Rohde, M.4    Mirold, S.5    Hardt, W.D.6
  • 25
    • 0035823591 scopus 로고    scopus 로고
    • SopE and SopE2 from Salmonella typhimurium activate different sets of Rho GTPases of the host cell
    • Friebel, A., Ilchmann, H., Aelpfelbacher, M., Ehrbar, K., Machleidt, W. and Hardt, W. D. (2001) SopE and SopE2 from Salmonella typhimurium activate different sets of Rho GTPases of the host cell. J. Biol. Chem. 276, 34035-34040
    • (2001) J. Biol. Chem , vol.276 , pp. 34035-34040
    • Friebel, A.1    Ilchmann, H.2    Aelpfelbacher, M.3    Ehrbar, K.4    Machleidt, W.5    Hardt, W.D.6
  • 26
    • 0036646473 scopus 로고    scopus 로고
    • Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
    • Buchwald, G., Friebel, A., Galàn, J. E., Hardt, W. D., Wittinghofer, A. and Scheffzek, K. (2002) Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE. EMBO J. 21, 3286-3295
    • (2002) EMBO J , vol.21 , pp. 3286-3295
    • Buchwald, G.1    Friebel, A.2    Galàn, J.E.3    Hardt, W.D.4    Wittinghofer, A.5    Scheffzek, K.6
  • 27
    • 4644371316 scopus 로고    scopus 로고
    • Solution structure, backbone dynamics, and interaction with Cdc42 of Salmonella guanine nucleotide exchange factor SopE2
    • Williams, C., Galyov, E. E. and Bagby, S. (2004) Solution structure, backbone dynamics, and interaction with Cdc42 of Salmonella guanine nucleotide exchange factor SopE2. Biochemistry 43, 11998-12008
    • (2004) Biochemistry , vol.43 , pp. 11998-12008
    • Williams, C.1    Galyov, E.E.2    Bagby, S.3
  • 29
    • 0036263915 scopus 로고    scopus 로고
    • Snyder, J. T., Worthylake, D. K., Rossman, K. L., Betts, L., Pruitt, W. M., Siderovski, D. P., Der, C. J. and Sondek, J. (2002) Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat. Struct. Biol. 9, 468-475
    • Snyder, J. T., Worthylake, D. K., Rossman, K. L., Betts, L., Pruitt, W. M., Siderovski, D. P., Der, C. J. and Sondek, J. (2002) Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat. Struct. Biol. 9, 468-475
  • 30
    • 33845800991 scopus 로고    scopus 로고
    • Capturing cyclic nucleotides in action: Snapshots from crystallographic studies
    • Rehmann, H., Wittinghofer, A. and Bos, J. L. (2007) Capturing cyclic nucleotides in action: snapshots from crystallographic studies. Nat. Rev. Mol. Cell Biol. 8, 63-73
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 63-73
    • Rehmann, H.1    Wittinghofer, A.2    Bos, J.L.3
  • 33
    • 5444271914 scopus 로고    scopus 로고
    • 15N resonances of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei
    • 15N resonances of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei. J. Biomol. NMR 29, 215-216
    • (2004) J. Biomol. NMR , vol.29 , pp. 215-216
    • Wu, H.-L.1    Williams, C.2    Upadhyay, A.3    Galyov, E.E.4    Bagby, S.5
  • 34
    • 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
  • 35
    • 42649116541 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 36
    • 84915716471 scopus 로고
    • Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura, S. and Ernst, R. R. (1980) Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy. J. Phys. 41, 95-117
    • (1980) J. Phys , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 37
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed-field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed-field gradient NMR techniques. J. Biomol. NMR 4, 845-858
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.W.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 39
    • 0035692486 scopus 로고    scopus 로고
    • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles
    • Chou, J. J., Gaemers, S., Howder, B., Louis, J. M. and Bax, A. (2001) A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. J. Biomol. NMR 21, 377-382
    • (2001) J. Biomol. NMR , vol.21 , pp. 377-382
    • Chou, J.J.1    Gaemers, S.2    Howder, B.3    Louis, J.M.4    Bax, A.5
  • 40
    • 0032042263 scopus 로고    scopus 로고
    • Ottiger, M., Delaglio, F. and Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 131, 373-378
    • Ottiger, M., Delaglio, F. and Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 131, 373-378
  • 41
    • 0027383637 scopus 로고    scopus 로고
    • 1H NMR. Proteins: Struct. Funct. Genet. 17, 297-309
    • 1H NMR. Proteins: Struct. Funct. Genet. 17, 297-309
  • 42
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 45
    • 0035742163 scopus 로고    scopus 로고
    • The VMD-Xplor visualization package for NMR structure refinement
    • Schwieters, C. D. and Clore, G. M. (2001) The VMD-Xplor visualization package for NMR structure refinement. J. Magn. Reson. 149, 239-244
    • (2001) J. Magn. Reson , vol.149 , pp. 239-244
    • Schwieters, C.D.1    Clore, G.M.2
  • 46
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R. and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 47
    • 0032748576 scopus 로고    scopus 로고
    • Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for Rho GTPases
    • Rudolph, M. G., Weise, C., Mirold, S., Hillenbrand, B., Bader, B., Wittinghofer, A. and Hardt, W. D. (1999) Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for Rho GTPases. J. Biol. Chem. 274, 30501-30509
    • (1999) J. Biol. Chem , vol.274 , pp. 30501-30509
    • Rudolph, M.G.1    Weise, C.2    Mirold, S.3    Hillenbrand, B.4    Bader, B.5    Wittinghofer, A.6    Hardt, W.D.7
  • 49
    • 0029118307 scopus 로고
    • Measurement of intrinsic nucleotide exchange and GTP hydrolysis rates
    • Self, A. J. and Hall, A. (1995) Measurement of intrinsic nucleotide exchange and GTP hydrolysis rates. Methods Enzymol. 256, 67-76
    • (1995) Methods Enzymol , vol.256 , pp. 67-76
    • Self, A.J.1    Hall, A.2
  • 50
    • 0032577563 scopus 로고    scopus 로고
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R. and Galàn, J. E. (1998) S. Typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R. and Galàn, J. E. (1998) S. Typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826
  • 51
    • 0033777306 scopus 로고    scopus 로고
    • Purification and biochemical activity of Salmonella exchange factor SopE
    • Friebel, A. and Hardt, W. D. (2000) Purification and biochemical activity of Salmonella exchange factor SopE. Meth. Enzymol. 325, 82-91
    • (2000) Meth. Enzymol , vol.325 , pp. 82-91
    • Friebel, A.1    Hardt, W.D.2
  • 52
    • 33846027894 scopus 로고    scopus 로고
    • Structural evidence for a common intermediate in small G protein-GEF reactions
    • Thomas, C., Fricke, I., Scrima, A., Berken, A. and Wittinghofer, A. (2007) Structural evidence for a common intermediate in small G protein-GEF reactions. Mol. Cell 25, 141-149
    • (2007) Mol. Cell , vol.25 , pp. 141-149
    • Thomas, C.1    Fricke, I.2    Scrima, A.3    Berken, A.4    Wittinghofer, A.5


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