메뉴 건너뛰기




Volumn 289, Issue 6, 2014, Pages 3591-3601

Membrane and Chaperone recognition by the major Translocator Protein PopB of the Type III secretion system of Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; HOST-PATHOGEN INTERACTIONS; MEMBRANE PROTEINS; PSEUDOMONAS AERUGINOSA; TYPE III SECRETION SYSTEM;

EID: 84893644126     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.517920     Document Type: Article
Times cited : (28)

References (55)
  • 1
    • 33750110911 scopus 로고    scopus 로고
    • The type iii secretion injectisome
    • Cornelis, G. R. (2006) The type III secretion injectisome. Nat. Rev. Microbiol. 4, 811-825
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 5
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane atpase during flagellar type iii protein export
    • Thomas, J., Stafford, G. P., and Hughes, C. (2004) Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export. Proc. Natl. Acad. Sci. U.S.A. 101, 3945-3950
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 6
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type iii secretion
    • Akeda, Y., and Galán, 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    Galán, J.E.2
  • 7
    • 84878241251 scopus 로고    scopus 로고
    • Substrate-Activated conformational switch on chaperones encodes a targeting signal in type iii secretion
    • Chen, L., Ai, X., Portaliou, A. G., Minetti, C. A., Remeta, D. P., Economou, A., and Kalodimos, C. G. (2013) Substrate-Activated conformational switch on chaperones encodes a targeting signal in type III secretion. Cell Rep. 3, 709-715
    • (2013) Cell Rep. , vol.3 , pp. 709-715
    • Chen, L.1    Ai, X.2    Portaliou, A.G.3    Minetti, C.A.4    Remeta, D.P.5    Economou, A.6    Kalodimos, C.G.7
  • 8
    • 77954407664 scopus 로고    scopus 로고
    • Structural basis of chaperone recognition by type iii secretion system minor translocator proteins
    • Job, V., Matteï, P.-J., Lemaire, D., Attree, I., and Dessen, A. (2010) Structural basis of chaperone recognition by type III secretion system minor translocator proteins, J. Biol. Chem. 285, 23224-23232
    • (2010) J. Biol. Chem. , vol.285 , pp. 23224-23232
    • Job, V.1    Matteï, P.-J.2    Lemaire, D.3    Attree, I.4    Dessen, A.5
  • 9
    • 70350455913 scopus 로고    scopus 로고
    • Functional characterization of ssae, a novel chaperone protein of the type iii secretion system encoded by salmonella pathogenicity island 2
    • Miki, T., Shibagaki, Y., Danbara, H., and Okada, N. (2009) Functional characterization of SsaE, a novel chaperone protein of the type III secretion system encoded by Salmonella pathogenicity island 2. J. Bacteriol. 191, 6843-6854
    • (2009) J. Bacteriol. , vol.191 , pp. 6843-6854
    • Miki, T.1    Shibagaki, Y.2    Danbara, H.3    Okada, N.4
  • 12
    • 69249157248 scopus 로고    scopus 로고
    • The type iii secretion system of pseudomonas aeruginosa. Infection by injection
    • Hauser, A. R. (2009) The type III secretion system of Pseudomonas aeruginosa. Infection by injection., Nat. Rev. Microbiol. 7, 654-665
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 654-665
    • Hauser, A.R.1
  • 13
    • 34547156156 scopus 로고    scopus 로고
    • Interaction between innate immune cells and a bacterial type iii secretion system in mutualistic and pathogenic associations
    • Silver, A. C., Kikuchi, Y., Fadl, A. A., Sha, J., Chopra, A. K., and Graf, J. (2007) Interaction between innate immune cells and a bacterial type III secretion system in mutualistic and pathogenic associations. Proc. Natl. Acad. Sci. U.S.A. 104, 9481-9486
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9481-9486
    • Silver, A.C.1    Kikuchi, Y.2    Fadl, A.A.3    Sha, J.4    Chopra, A.K.5    Graf, J.6
  • 14
    • 77955352032 scopus 로고    scopus 로고
    • Chromobacterium pathogenicity island 1 type iii secretion system is a major virulence determinant for chromobacterium violaceum-induced cell death in hepatocytes
    • Miki, T., Iguchi, M., Akiba, K., Hosono, M., Sobue, T., Danbara, H., and Okada, N. (2010) Chromobacterium pathogenicity island 1 type III secretion system is a major virulence determinant for Chromobacterium violaceum-induced cell death in hepatocytes. Mol. Microbiol. 77, 855-872
    • (2010) Mol. Microbiol. , vol.77 , pp. 855-872
    • Miki, T.1    Iguchi, M.2    Akiba, K.3    Hosono, M.4    Sobue, T.5    Danbara, H.6    Okada, N.7
  • 17
    • 33947249049 scopus 로고    scopus 로고
    • The type iii secretion system needle tip complex mediates host cell sensing and translocon insertion
    • Veenendaal, A. K., Hodgkinson, J. L., Schwarzer, L., Stabat, D., Zenk, S. F., and Blocker, A. J. (2007) The type III secretion system needle tip complex mediates host cell sensing and translocon insertion. Mol. Microbiol. 63, 1719-1730
    • (2007) Mol. Microbiol. , vol.63 , pp. 1719-1730
    • Veenendaal, A.K.1    Hodgkinson, J.L.2    Schwarzer, L.3    Stabat, D.4    Zenk, S.F.5    Blocker, A.J.6
  • 18
    • 33745279057 scopus 로고    scopus 로고
    • Assembly of the inner rod determines needle length in the type iii secretion injectisome
    • Marlovits, T. C., Kubori, T., Lara-Tejero, M., Thomas, D., Unger, V. M., and Galán, J. E. (2006) Assembly of the inner rod determines needle length in the type III secretion injectisome. Nature 441, 637-640
    • (2006) Nature , Issue.441 , pp. 637-640
    • Marlovits, T.C.1    Kubori, T.2    Lara-Tejero, M.3    Thomas, D.4    Unger, V.5    Galán, J.6
  • 19
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type iii secretion needle complex
    • Marlovits, T. C., Kubori, T., Sukhan, A., Thomas, D. R., Galán, J. E., and Unger, V. M. (2004) Structural insights into the assembly of the type III secretion needle complex. Science 306, 1040-1042
    • (2004) Science , Issue.306 , pp. 1040-1042
    • Marlovits, T.C.1    Kubori, T.2    Sukhan, A.3    Thomas, D.R.4    Galán, J.E.5    Unger, V.6
  • 22
    • 78751651347 scopus 로고    scopus 로고
    • Membrane targeting and pore formation by the type iii secretion system translocon
    • Matteï, P.-J., Faudry, E., Job, V., Izoré, T., Attree, I., and Dessen, A. (2011) Membrane targeting and pore formation by the type III secretion system translocon. FEBS J. 278, 414-426
    • (2011) FEBS J. , vol.278 , pp. 414-426
    • Matteï, P.-J.1    Faudry, E.2    Job, V.3    Izoré, T.4    Attree, I.5    Dessen, A.6
  • 23
    • 84864200181 scopus 로고    scopus 로고
    • The pseudomonas aeruginosa type iii secretion system has an exotoxin s/t/y independent pathogenic role during acute lung infection
    • Galle, M., Jin, S., Bogaert, P., Haegman, M., Vandenabeele, P., and Beyaert, R. (2012) The Pseudomonas aeruginosa type III secretion system has an exotoxin S/T/Y independent pathogenic role during acute lung infection. PLoS ONE 7, e41547
    • (2012) PLoS ONE , vol.7
    • Galle, M.1    Jin, S.2    Bogaert, P.3    Haegman, M.4    Vandenabeele, P.5    Beyaert, R.6
  • 24
    • 0035047787 scopus 로고    scopus 로고
    • Poreforming activity of type iii system-secreted proteins leads to oncosis of pseudomonas aeruginosa-infected macrophages
    • Dacheux, D., Goure, J., Chabert, J., Usson, Y., and Attree, I. (2001) Poreforming activity of type III system-secreted proteins leads to oncosis of Pseudomonas aeruginosa-infected macrophages. Mol. Microbiol. 40, 76-85
    • (2001) Mol. Microbiol. , vol.40 , pp. 76-85
    • Dacheux, D.1    Goure, J.2    Chabert, J.3    Usson, Y.4    Attree, I.5
  • 25
    • 0037380681 scopus 로고    scopus 로고
    • Protein binding between pcrg-pcrv and pcrhpopb/popd encoded by the pcrgvh-popbd operon of the pseudomonas aeruginosa type iii secretion system
    • Allmond, L. R., Karaca, T. J., Nguyen, V. N., Nguyen, T., Wiener-Kronish, J. P., and Sawa, T. (2003) Protein binding between PcrG-PcrV and PcrHPopB/PopD encoded by the pcrGVH-popBD operon of the Pseudomonas aeruginosa type III secretion system. Infect Immun 71, 2230-2233
    • (2003) Infect Immun , vol.71 , pp. 2230-2233
    • Allmond, L.R.1    Karaca, T.J.2    Nguyen, V.N.3    Nguyen, T.4    Wiener-Kronish, J.P.5    Sawa, T.6
  • 26
    • 0141642035 scopus 로고    scopus 로고
    • Oligomerization of type iii secretion proteins popb and popd precedes pore formation in pseudomonas
    • Schoehn, G., Di Guilmi, A. M., Lemaire, D., Attree, I., Weissenhorn, W., and Dessen, A. (2003) Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas. EMBO J. 22, 4957-4967
    • (2003) EMBO J. , vol.22 , pp. 4957-4967
    • Schoehn, G.1    Di Guilmi, A.M.2    Lemaire, D.3    Attree, I.4    Weissenhorn, W.5    Dessen, A.6
  • 27
    • 59849110833 scopus 로고    scopus 로고
    • Role of pseudomonas aeruginosa type iii effectors in disease
    • Engel, J., and Balachandran, P. (2009) Role of Pseudomonas aeruginosa type III effectors in disease. Curr. Opin. Microbiol. 12, 61-66
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 61-66
    • Engel, J.1    Balachandran, P.2
  • 28
    • 0032060962 scopus 로고    scopus 로고
    • Improved cross-peak detection in two-dimensional protonnmrspectra using excitation sculpting
    • Van, Q. N., and Shaka, A. J. (1998) Improved cross-peak detection in two-dimensional protonNMRspectra using excitation sculpting. J. Magn. Reson. 132, 154-158
    • (1998) J. Magn. Reson. , vol.132 , pp. 154-158
    • Van, Q.N.1    Shaka, A.J.2
  • 29
    • 0024368864 scopus 로고
    • Precise gene fusion by pcr
    • Yon, J., and Fried, M. (1989) Precise gene fusion by PCR. Nucleic Acids Res. 17, 4895
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4895
    • Yon, J.1    Fried, M.2
  • 30
    • 84856405338 scopus 로고    scopus 로고
    • Injection of pseudomonas aeruginosa exo toxins into host cells can be modulated by host factors at the level of translocon assembly and/or activity
    • Verove, J., Bernarde, C., Bohn, Y. S., Boulay, F., Rabiet, M. J., Attree, I., and Cretin, F. (2012) Injection of Pseudomonas aeruginosa Exo toxins into host cells can be modulated by host factors at the level of translocon assembly and/or activity. PLoS ONE 7, e30488
    • (2012) PLoS ONE , vol.7
    • Verove, J.1    Bernarde, C.2    Bohn, Y.S.3    Boulay, F.4    Rabiet, M.J.5    Attree, I.6    Cretin, F.7
  • 35
    • 0032922193 scopus 로고    scopus 로고
    • Sfcheck. A unified set of procedure for evaluating the quality of macromolecular structurefactor data and their agreement with atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK. A unified set of procedure for evaluating the quality of macromolecular structurefactor data and their agreement with atomic model. Acta Crystallogr. D Biol. Crystallogr. 55, 191-205
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 37
    • 0032478191 scopus 로고    scopus 로고
    • Receptor-triggered membrane association of model retroviral glycoprotein
    • Damico, R. L., Crane, J., and Bates, P. (1998) Receptor-triggered membrane association of model retroviral glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 95, 2580-2585
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2580-2585
    • Damico, R.L.1    Crane, J.2    Bates, P.3
  • 39
    • 0033230438 scopus 로고    scopus 로고
    • The tripartite type iii secreton of shigella flexneri inserts ipab and ipac into host membranes
    • Blocker, A., Gounon, P., Larquet, E., Niebuhr, K., Cabiaux, V., Parsot, C., and Sansonetti, P. (1999) The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 147, 683-693
    • (1999) J. Cell Biol. , vol.147 , pp. 683-693
    • Blocker, A.1    Gounon, P.2    Larquet, E.3    Niebuhr, K.4    Cabiaux, V.5    Parsot, C.6    Sansonetti, P.7
  • 40
    • 0036015644 scopus 로고    scopus 로고
    • Topology of the salmonella invasion protein sipb in a model bilayer
    • McGhie, E. J., Hume, P. J., Hayward, R. D., Torres, J., and Koronakis, V. (2002) Topology of the Salmonella invasion protein SipB in a model bilayer. Mol. Microbiol. 44, 1309-1321
    • (2002) Mol. Microbiol. , vol.44 , pp. 1309-1321
    • McGhie, E.J.1    Hume, P.J.2    Hayward, R.D.3    Torres, J.4    Koronakis, V.5
  • 41
    • 16244414595 scopus 로고    scopus 로고
    • Role of predicted transmembrane domains for type iii translocation, pore formation, and signaling by the yersinia pseudotuberculosis yopb protein
    • Ryndak, M. B., Chung, H., London, E., and Bliska, J. B. (2005) Role of predicted transmembrane domains for type III translocation, pore formation, and signaling by the Yersinia pseudotuberculosis YopB protein. Infect. Immun. 73, 2433-2443
    • (2005) Infect. Immun. , vol.73 , pp. 2433-2443
    • Ryndak, M.B.1    Chung, H.2    London, E.3    Bliska, J.B.4
  • 42
    • 0038501071 scopus 로고    scopus 로고
    • The purified shigella ipab and salmonella sipb translocators share biochemical properties and membrane topology
    • Hume, P. J., McGhie, E. J., Hayward, R. D., and Koronakis, V. (2003) The purified Shigella IpaB and Salmonella SipB translocators share biochemical properties and membrane topology. Mol. Microbiol. 49, 425-439
    • (2003) Mol. Microbiol. , vol.49 , pp. 425-439
    • Hume, P.J.1    McGhie, E.J.2    Hayward, R.D.3    Koronakis, V.4
  • 44
    • 80051719676 scopus 로고    scopus 로고
    • Efficient isolation of pseudomonas aeruginosa type iii secretion translocators and assembly of heteromeric transmembrane pores in model membranes
    • Romano, F. B., Rossi, K. C., Savva, C. G., Holzenburg, A., Clerico, E. M., and Heuck, A. P. (2011) Efficient isolation of Pseudomonas aeruginosa type III secretion translocators and assembly of heteromeric transmembrane pores in model membranes. Biochemistry 50, 7117-7131
    • (2011) Biochemistry , vol.50 , pp. 7117-7131
    • Romano, F.B.1    Rossi, K.C.2    Savva, C.G.3    Holzenburg, A.4    Clerico, E.M.5    Heuck, A.P.6
  • 45
    • 33745615443 scopus 로고    scopus 로고
    • Synergistic pore formation by type iii toxin translocators of pseudomonas aeruginosa
    • Faudry, E., Vernier, G., Neumann, E., Forge, V., and Attree, I. (2006) Synergistic pore formation by type III toxin translocators of Pseudomonas aeruginosa. Biochemistry 45, 8117-8123
    • (2006) Biochemistry , vol.45 , pp. 8117-8123
    • Faudry, E.1    Vernier, G.2    Neumann, E.3    Forge, V.4    Attree, I.5
  • 46
    • 34447327540 scopus 로고    scopus 로고
    • Type iii secretion system translocator has a molten globule conformation both in its free and chaperone-bound forms
    • Faudry, E., Job, V., Dessen, A., Attree, I., and Forge, V. (2007) Type III secretion system translocator has a molten globule conformation both in its free and chaperone-bound forms. FEBS J. 274, 3601-3610
    • (2007) FEBS J. , vol.274 , pp. 3601-3610
    • Faudry, E.1    Job, V.2    Dessen, A.3    Attree, I.4    Forge, V.5
  • 49
    • 3343006984 scopus 로고    scopus 로고
    • The v antigen of pseudomonas aeruginosa is required for assembly of the functional popb/popd translocation pore in host cell membranes
    • Goure, J., Pastor, A., Faudry, E., Chabert, J., Dessen, A., and Attree, I. (2004) The V antigen of Pseudomonas aeruginosa is required for assembly of the functional PopB/PopD translocation pore in host cell membranes. Infect. Immun. 72, 4741-4750
    • (2004) Infect. Immun. , vol.72 , pp. 4741-4750
    • Goure, J.1    Pastor, A.2    Faudry, E.3    Chabert, J.4    Dessen, A.5    Attree, I.6
  • 50
    • 67649861394 scopus 로고    scopus 로고
    • Ipabipgc interaction defines binding motif for type iii secretion translocator
    • Lunelli, M., Lokareddy, R. K., Zychlinsky, A., and Kolbe, M. (2009) IpaBIpgC interaction defines binding motif for type III secretion translocator. Proc. Natl. Acad. Sci. U.S.A. 106, 9661-9666
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9661-9666
    • Lunelli, M.1    Lokareddy, R.K.2    Zychlinsky, A.3    Kolbe, M.4
  • 51
    • 78650063483 scopus 로고    scopus 로고
    • Combination of two separate binding domains defines stoichiometry between type iii secretion system chaperone ipgc and translocator protein ipab
    • Lokareddy, R. K., Lunelli, M., Eilers, B., Wolter, V., and Kolbe, M. (2010) Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB. J. Biol. Chem. 285, 39965-39975
    • (2010) J. Biol. Chem. , vol.285 , pp. 39965-39975
    • Lokareddy, R.K.1    Lunelli, M.2    Eilers, B.3    Wolter, V.4    Kolbe, M.5
  • 52
    • 84862268306 scopus 로고    scopus 로고
    • Crystal structure of the yersinia enterocolitica type iii secretion chaperone sycd in complex with a peptide of the minor translocator yopd
    • Schreiner, M., and Niemann, H. H. (2012) Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Struct. Biol. 12, 13
    • (2012) BMC Struct. Biol. , vol.12 , pp. 13
    • Schreiner, M.1    Niemann, H.H.2
  • 53
    • 84885962359 scopus 로고    scopus 로고
    • Dimerization of the p. Aeruginosa translocator chaperone pcrh is required for stability not function
    • Tomalka, A. G., Zmina, S. E., Stopford, C. M., and Rietsch, A. (2013) Dimerization of the P. aeruginosa translocator chaperone PcrH is required for stability not function. J. Bacteriol. 195, 4836-4843
    • (2013) J. Bacteriol. , vol.195 , pp. 4836-4843
    • Tomalka, A.G.1    Zmina, S.E.2    Stopford, C.M.3    Rietsch, A.4
  • 54
    • 77955495219 scopus 로고    scopus 로고
    • Yopd self-Assembly and binding to lcrv facilitate type iii secretion activity by yersinia pseudotuberculosis
    • Costa, T. R., Edqvist, P. J., Bröms, J. E., Ahlund, M. K., Forsberg, A., and Francis, M. S. (2010) YopD self-Assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis. J. Biol. Chem. 285, 25269-25284
    • (2010) J. Biol. Chem. , vol.285 , pp. 25269-25284
    • Costa, T.R.1    Edqvist, P.J.2    Bröms, J.E.3    Ahlund, M.K.4    Forsberg, A.5    Francis, M.S.6
  • 55
    • 0030915704 scopus 로고    scopus 로고
    • Improved r-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs, K., and Karplus, P. A. (1997) Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat. Struct. Biol. 4, 269-275
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.