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Volumn 185, Issue 24, 2003, Pages 7279-7284

InvB Is a Type III Secretion-Associated Chaperone for the Salmonella enterica Effector Protein SopE

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEIN INVB; PROTEIN SOPE; UNCLASSIFIED DRUG;

EID: 0344666692     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.24.7279-7284.2003     Document Type: Article
Times cited : (34)

References (34)
  • 1
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan, S. C., R. M. Phillips, and P. Ghosh. 2002. Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol. Cell 9:971-980.
    • (2002) Mol. Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 2
    • 0034462757 scopus 로고    scopus 로고
    • InvB is a type III secretion chaperone specific for SspA
    • Bronstein, P. A., E. A. Miao, and S. I. Miller. 2000. InvB is a type III secretion chaperone specific for SspA. J. Bacteriol. 182:6638-6644.
    • (2000) J. Bacteriol. , vol.182 , pp. 6638-6644
    • Bronstein, P.A.1    Miao, E.A.2    Miller, S.I.3
  • 3
    • 0036646473 scopus 로고    scopus 로고
    • Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
    • Buchwald, G., A. Friebel, J. E. Galán, W. D. Hardt, A. Wittinghofer, and K. Scheffzek. 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    Galán, J.E.3    Hardt, W.D.4    Wittinghofer, A.5    Scheffzek, K.6
  • 4
    • 0033943054 scopus 로고    scopus 로고
    • LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism
    • Cambronne, E. D., L. W. Cheng, and O. Schneewind. 2000. LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism. Mol. Microbiol. 37:263-273.
    • (2000) Mol. Microbiol. , vol.37 , pp. 263-273
    • Cambronne, E.D.1    Cheng, L.W.2    Schneewind, O.3
  • 5
    • 0029818081 scopus 로고    scopus 로고
    • Salmonella spp. are cytotoxic for cultured macrophages
    • Chen, L. M., K. Kaniga, and J. E. Galán. 1996. Salmonella spp. are cytotoxic for cultured macrophages. Mol. Microbiol. 21:1101-1115.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1101-1115
    • Chen, L.M.1    Kaniga, K.2    Galán, J.E.3
  • 6
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis, G. R., and F. Van Gijsegem. 2000. Assembly and function of type III secretory systems. Annu. Rev. Microbiol. 54:735-774.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 7
    • 0035901560 scopus 로고    scopus 로고
    • Type III secretion chaperone-dependent regulation: Activation of virulence genes by SicA and InvF in Salmonella typhimurium
    • Darwin, K., and V. Miller. 2001. Type III secretion chaperone-dependent regulation: activation of virulence genes by SicA and InvF in Salmonella typhimurium. EMBO J. 20:1850-1862.
    • (2001) EMBO J. , vol.20 , pp. 1850-1862
    • Darwin, K.1    Miller, V.2
  • 8
    • 0032765129 scopus 로고    scopus 로고
    • Differential regulation of Salmonella typhimurium type III secreted proteins by pathogenicity island 1 (SPI-1)-encoded transcriptional activators InvF and HilA
    • Eichelberg, K., and J. E. Galan. 1999. Differential regulation of Salmonella typhimurium type III secreted proteins by pathogenicity island 1 (SPI-1)-encoded transcriptional activators InvF and HilA. Infect Immun. 67:4099-4105.
    • (1999) Infect Immun. , vol.67 , pp. 4099-4105
    • Eichelberg, K.1    Galan, J.E.2
  • 11
    • 0031801744 scopus 로고    scopus 로고
    • Identification of a specific chaperone for SptP, a substrate of the centisome 63 type III secretion system of Salmonella typhimurium
    • Fu, Y., and J. E. Galán. 1998. Identification of a specific chaperone for SptP, a substrate of the centisome 63 type III secretion system of Salmonella typhimurium. J. Bacteriol. 180:3393-3399.
    • (1998) J. Bacteriol. , vol.180 , pp. 3393-3399
    • Fu, Y.1    Galán, J.E.2
  • 12
    • 0035188434 scopus 로고    scopus 로고
    • Salmonella interaction with host cells: Type III secretion at work
    • Galán, J. E. 2001. Salmonella interaction with host cells: type III secretion at work. Annu. Rev. Cell Dev. Biol. 17:53-86.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 53-86
    • Galán, J.E.1
  • 13
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • Galán, J. E., and A. Collmer. 1999. Type III secretion machines: bacterial devices for protein delivery into host cells. Science 294:1322-1328.
    • (1999) Science , vol.294 , pp. 1322-1328
    • Galán, J.E.1    Collmer, A.2
  • 14
    • 0024323292 scopus 로고
    • Cloning and molecular characterization of genes whose products allow Salmonella typhimurium to penetrate tissue culture cells
    • Galán, J. E., and R. Curtiss III. 1989. Cloning and molecular characterization of genes whose products allow Salmonella typhimurium to penetrate tissue culture cells. Proc. Natl. Acad. Sci. USA 86;6383-6387.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6383-6387
    • Galán, J.E.1    Curtiss III, R.2
  • 15
    • 0034255340 scopus 로고    scopus 로고
    • Striking a balance: Modulation of the actin cytoskeleton by Salmonella
    • Galán, J. E., and D. Zhou. 2000. Striking a balance: modulation of the actin cytoskeleton by Salmonella. Proc. Natl. Acad. Sci. USA 97:8754-8761.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8754-8761
    • Galán, J.E.1    Zhou, D.2
  • 16
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 17
    • 0032577563 scopus 로고    scopus 로고
    • Salmonella typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • Hardt, W.-D., L.-M. Chen, K. E. Schuebel, X. R. Bustelo, and J. E. Galán. 1998. Salmonella typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93:815-826.
    • (1998) Cell , vol.93 , pp. 815-826
    • Hardt, W.-D.1    Chen, L.-M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galán, J.E.5
  • 18
    • 0032478074 scopus 로고    scopus 로고
    • A target of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage
    • Hardt, W.-D., H. Urlaub, and J. E. Galán. 1998. A target of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage. Proc. Natl. Acad. Sci. USA 95:2574-2579.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2574-2579
    • Hardt, W.-D.1    Urlaub, H.2    Galán, J.E.3
  • 19
    • 0031682153 scopus 로고    scopus 로고
    • YscB of Yersinia pestis functions as a specific chaperone for YopN
    • Jackson, M., J. Day, and G. Plano. 1998. YscB of Yersinia pestis functions as a specific chaperone for YopN. J. Bacteriol. 180:4912-4921.
    • (1998) J. Bacteriol. , vol.180 , pp. 4912-4921
    • Jackson, M.1    Day, J.2    Plano, G.3
  • 20
    • 0027982037 scopus 로고
    • The Salmonella typhimurium invasion genes invF and invG encode homologues to the PulD and AraC family of proteins
    • Kaniga, K., J. C. Bossio, and J. E. Galán. 1994. The Salmonella typhimurium invasion genes invF and invG encode homologues to the PulD and AraC family of proteins. Mol. Microbiol. 13:555-568.
    • (1994) Mol. Microbiol. , vol.13 , pp. 555-568
    • Kaniga, K.1    Bossio, J.C.2    Galán, J.E.3
  • 21
    • 0028113512 scopus 로고
    • Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri
    • Ménard, R., P. J. Sansonetti, C. Parsot, and T. Vasselon. 1994. Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri. Cell 79:515-529.
    • (1994) Cell , vol.79 , pp. 515-529
    • Ménard, R.1    Sansonetti, P.J.2    Parsot, C.3    Vasselon, T.4
  • 23
    • 0027976793 scopus 로고
    • The adenovirus E4-6/7 protein transactivates the E2 promoter by inducing dimerization of a heteromeric E2F complex
    • Obert, S., R. J. O'Connor, S. Schmid, and P. Hearing. 1994. The adenovirus E4-6/7 protein transactivates the E2 promoter by inducing dimerization of a heteromeric E2F complex. Mol. Cell. Biol. 14:1333-1346.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1333-1346
    • Obert, S.1    O'Connor, R.J.2    Schmid, S.3    Hearing, P.4
  • 24
    • 0036032109 scopus 로고    scopus 로고
    • Chaperones of the type III secretion pathway: Jacks of all trades
    • Page, A. L., and C. Parsot. 2002. Chaperones of the type III secretion pathway: jacks of all trades. Mol. Microbiol. 46:1-11.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1-11
    • Page, A.L.1    Parsot, C.2
  • 25
    • 0028802323 scopus 로고
    • Cell surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell
    • Persson, C., R. Nordfelth, A. Holmström, S. Hakansson, R. Rosqvist, and H. Wolf-Watz. 1995. Cell surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell. Mol. Microbiol. 18:135-150.
    • (1995) Mol. Microbiol. , vol.18 , pp. 135-150
    • Persson, C.1    Nordfelth, R.2    Holmström, A.3    Hakansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 26
    • 0345421685 scopus 로고    scopus 로고
    • Priming virulence factors for delivery into the host
    • in press
    • Stebbins, C. E., and J. E. Galan. Priming virulence factors for delivery into the host. Nat. Rev. Mol. Biol., in press.
    • Nat. Rev. Mol. Biol.
    • Stebbins, C.E.1    Galan, J.E.2
  • 27
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C. E., and J. E. Galán. 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    Galán, J.E.2
  • 28
    • 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., A. Friebel, S. Linder, M. Rohde, S. Mirold, and W. D. Hardt. 2000. Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell. Mol. Microbiol. 36:1206-1211.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1206-1211
    • Stender, S.1    Friebel, A.2    Linder, S.3    Rohde, M.4    Mirold, S.5    Hardt, W.D.6
  • 29
    • 0034079727 scopus 로고    scopus 로고
    • Complex function for SicA, a Salmonella enterica serovar Typhimurium type III secretion-associated chaperone
    • Tucker, S. C., and J. E. Galán. 2000. Complex function for SicA, a Salmonella enterica serovar Typhimurium type III secretion-associated chaperone. J. Bacteriol. 182:2262-2268.
    • (2000) J. Bacteriol. , vol.182 , pp. 2262-2268
    • Tucker, S.C.1    Galán, J.E.2
  • 31
    • 0027499076 scopus 로고
    • SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE
    • Wattiau, P., and G. R. Cornelis. 1993. SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE. Mol. Microbiol. 8:123-131.
    • (1993) Mol. Microbiol. , vol.8 , pp. 123-131
    • Wattiau, P.1    Cornelis, G.R.2
  • 32
    • 0029886432 scopus 로고    scopus 로고
    • Customized secretion chaperones in pathogenic bacteria
    • Wattiau, P., S. Woestyn, and G. R. Cornelis. 1996. Customized secretion chaperones in pathogenic bacteria. Mol. Microbiol. 20:255-262.
    • (1996) Mol. Microbiol. , vol.20 , pp. 255-262
    • Wattiau, P.1    Woestyn, S.2    Cornelis, G.R.3
  • 33
    • 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., R. Rosqvist, P. B. Mullan, M. H. Edwards, and E. E. Galyov. 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
  • 34
    • 0035147455 scopus 로고    scopus 로고
    • A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
    • Zhou, D., L. M. Chen, L. Hernandez, S. B. Shears, and J. E. Galán. 2001. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Mol. Microbiol. 39:248-259.
    • (2001) Mol. Microbiol. , vol.39 , pp. 248-259
    • Zhou, D.1    Chen, L.M.2    Hernandez, L.3    Shears, S.B.4    Galán, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.