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Volumn 12, Issue 12, 2016, Pages

Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus

(16)  Dietsche, Tobias a   Tesfazgi Mebrhatu, Mehari a   Brunner, Matthias J b,c,d   Abrusci, Patrizia e   Yan, Jun f,j   Franz Wachtel, Mirita a   Schärfe, Charlotta a   Zilkenat, Susann a   Grin, Iwan a   Galán, Jorge E g   Kohlbacher, Oliver a,h   Lea, Susan e   Macek, Boris a   Marlovits, Thomas C b,c,d   Robinson, Carol V f   Wagner, Samuel a,i  


Author keywords

[No Author keywords available]

Indexed keywords

MODEL; PERIPLASM; PROTEIN DOMAIN; SECRETORY PATHWAY; STRUCTURE ACTIVITY RELATION; ELECTRON MICROSCOPY; IMAGE PROCESSING; IMMUNOBLOTTING; MASS SPECTROMETRY; METABOLISM; SALMONELLA ENTERICA SEROVAR TYPHIMURIUM; SIZE EXCLUSION CHROMATOGRAPHY; TYPE III SECRETION SYSTEM; ULTRASTRUCTURE;

EID: 85007524055     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1006071     Document Type: Article
Times cited : (62)

References (58)
  • 1
    • 84907563228 scopus 로고    scopus 로고
    • Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells
    • 25002086,.;: –;
    • Galán JE, Lara-Tejero M, Marlovits TC, Wagner S, Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells. Annu Rev Microbiol. 2014;68: 415–;438. doi: 10.1146/annurev-micro-092412-15572525002086
    • (2014) Annu Rev Microbiol , vol.68 , pp. 415-438
    • Galán, J.E.1    Lara-Tejero, M.2    Marlovits, T.C.3    Wagner, S.4
  • 2
    • 34447099537 scopus 로고    scopus 로고
    • SnapShot: effector proteins of type III secretion systems
    • 17632065,.;: –;
    • Galán JE, SnapShot: effector proteins of type III secretion systems. Cell. 2007;130: 192–;192.e2. doi: 10.1016/j.cell.2007.06.04217632065
    • (2007) Cell , vol.130 , pp. 192-192.e2
    • Galán, J.E.1
  • 3
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • 21385715,.;: –;
    • Schraidt O, Marlovits TC, Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science. 2011;331: 1192–;1195. doi: 10.1126/science.119935821385715
    • (2011) Science , vol.331 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 4
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • 9554854,..;: –;
    • Kubori T, Matsushima Y, Nakamura D, Uralil J, Lara-Tejero M, Sukhan A, et al. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science. 1998;280: 602–;605. 9554854
    • (1998) Science , vol.280 , pp. 602-605
    • Kubori, T.1    Matsushima, Y.2    Nakamura, D.3    Uralil, J.4    Lara-Tejero, M.5    Sukhan, A.6
  • 5
    • 84893742076 scopus 로고    scopus 로고
    • Structure of a pathogenic type 3 secretion system in action
    • 24317488,.;: –;
    • Radics J, Königsmaier L, Marlovits TC, Structure of a pathogenic type 3 secretion system in action. Nat Struct Mol Biol. 2014;21: 82–;87. doi: 10.1038/nsmb.272224317488
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 82-87
    • Radics, J.1    Königsmaier, L.2    Marlovits, T.C.3
  • 6
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • 16208377,.;: –;
    • Akeda Y, Galán JE, Chaperone release and unfolding of substrates in type III secretion. Nature. 2005;437: 911–;915. doi: 10.1038/nature0399216208377
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galán, J.E.2
  • 7
    • 79952280754 scopus 로고    scopus 로고
    • A sorting platform determines the order of protein secretion in bacterial type III systems
    • 21292939,.;: –;
    • Lara-Tejero M, Kato J, Wagner S, Liu X, Galán JE, A sorting platform determines the order of protein secretion in bacterial type III systems. Science. 2011;331: 1188–;1191. doi: 10.1126/science.120147621292939
    • (2011) Science , vol.331 , pp. 1188-1191
    • Lara-Tejero, M.1    Kato, J.2    Wagner, S.3    Liu, X.4    Galán, J.E.5
  • 8
    • 0030701512 scopus 로고    scopus 로고
    • The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body
    • 9426140,.;: –;
    • Fan F, Ohnishi K, Francis NR, Macnab RM, The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body. Mol Microbiol. 1997;26: 1035–;1046. 9426140
    • (1997) Mol Microbiol , vol.26 , pp. 1035-1046
    • Fan, F.1    Ohnishi, K.2    Francis, N.R.3    Macnab, R.M.4
  • 10
    • 84906099584 scopus 로고    scopus 로고
    • Assembly and structure of the T3SS
    • 24512838,.;: –;
    • Burkinshaw BJ, Strynadka NCJ, Assembly and structure of the T3SS. Biochim Biophys Acta. 2014;1843: 1649–;1663. doi: 10.1016/j.bbamcr.2014.01.03524512838
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 1649-1663
    • Burkinshaw, B.J.1    Strynadka, N.C.J.2
  • 12
    • 84964702201 scopus 로고    scopus 로고
    • Determination of the stoichiometry of the complete bacterial type III secretion needle complex using a combined quantitative proteomic approach
    • Zilkenat S, Franz-Wachtel M, Stierhof Y-D, Galán JE, Macek B, Wagner S, Determination of the stoichiometry of the complete bacterial type III secretion needle complex using a combined quantitative proteomic approach. Molecular & Cellular Proteomics. 2016;15: 1598–;1609.
    • (2016) Molecular & Cellular Proteomics , vol.15 , pp. 1598-1609
    • Zilkenat, S.1    Franz-Wachtel, M.2    Stierhof, Y.-D.3    Galán, J.E.4    Macek, B.5    Wagner, S.6
  • 14
    • 77954224937 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA
    • 20306492,.;: –;
    • Worrall LJ, Vuckovic M, Strynadka NCJ, Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA. Protein Sci. 2010;19: 1091–;1096. doi: 10.1002/pro.38220306492
    • (2010) Protein Sci , vol.19 , pp. 1091-1096
    • Worrall, L.J.1    Vuckovic, M.2    Strynadka, N.C.J.3
  • 15
  • 16
    • 67549133101 scopus 로고    scopus 로고
    • Mutations in flk, flgG, flhA, and flhE that affect the flagellar type III secretion specificity switch in Salmonella enterica
    • 19376867,.;: –;
    • Hirano T, Mizuno S, Aizawa S-I, Hughes KT, Mutations in flk, flgG, flhA, and flhE that affect the flagellar type III secretion specificity switch in Salmonella enterica. J Bacteriol. 2009;191: 3938–;3949. doi: 10.1128/JB.01811-0819376867
    • (2009) J Bacteriol , vol.191 , pp. 3938-3949
    • Hirano, T.1    Mizuno, S.2    Aizawa, S.-I.3    Hughes, K.T.4
  • 18
    • 79960463317 scopus 로고    scopus 로고
    • Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA
    • 21811603,.;
    • Hara N, Namba K, Minamino T, Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA. PLoS ONE. 2011;6: e22417. doi: 10.1371/journal.pone.002241721811603
    • (2011) PLoS ONE , vol.6 , pp. e22417
    • Hara, N.1    Namba, K.2    Minamino, T.3
  • 19
    • 33750992443 scopus 로고    scopus 로고
    • Flipping the switch: bringing order to flagellar assembly
    • 17067800,.;: –;
    • Ferris HU, Minamino T, Flipping the switch: bringing order to flagellar assembly. Trends Microbiol. 2006;14: 519–;526. doi: 10.1016/j.tim.2006.10.00617067800
    • (2006) Trends Microbiol , vol.14 , pp. 519-526
    • Ferris, H.U.1    Minamino, T.2
  • 20
  • 21
    • 80053983313 scopus 로고    scopus 로고
    • The assembly of the export apparatus (YscR,S,T,U,V) of the Yersinia type III secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer
    • 21923772,.;: –;
    • Diepold A, Wiesand U, Cornelis GR, The assembly of the export apparatus (YscR,S,T,U,V) of the Yersinia type III secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer. Mol Microbiol. 2011;82: 502–;514. doi: 10.1111/j.1365-2958.2011.07830.x21923772
    • (2011) Mol Microbiol , vol.82 , pp. 502-514
    • Diepold, A.1    Wiesand, U.2    Cornelis, G.R.3
  • 22
    • 84903906434 scopus 로고    scopus 로고
    • Dynamics of expression and maturation of the type III secretion system of enteropathogenic Escherichia coli
    • 24837293,.;: –;
    • Yerushalmi G, Litvak Y, Gur-Arie L, Rosenshine I, Dynamics of expression and maturation of the type III secretion system of enteropathogenic Escherichia coli. J Bacteriol. 2014;196: 2798–;2806. doi: 10.1128/JB.00069-1424837293
    • (2014) J Bacteriol , vol.196 , pp. 2798-2806
    • Yerushalmi, G.1    Litvak, Y.2    Gur-Arie, L.3    Rosenshine, I.4
  • 23
    • 84904040058 scopus 로고    scopus 로고
    • Assembly of the bacterial type III secretion machinery
    • 24484471,.;: –;
    • Diepold A, Wagner S, Assembly of the bacterial type III secretion machinery. FEMS Microbiol Rev. 2014;38: 802–;822. doi: 10.1111/1574-6976.1206124484471
    • (2014) FEMS Microbiol Rev , vol.38 , pp. 802-822
    • Diepold, A.1    Wagner, S.2
  • 24
    • 0029846007 scopus 로고    scopus 로고
    • Requirement for exported proteins in secretion through the invasion-associated type III system of Salmonella typhimurium
    • 8751894,.;: –;
    • Collazo CM, Galan JE, Requirement for exported proteins in secretion through the invasion-associated type III system of Salmonella typhimurium. Infection and Immunity. 1996;64: 3524–;3531. 8751894
    • (1996) Infection and Immunity , vol.64 , pp. 3524-3531
    • Collazo, C.M.1    Galan, J.E.2
  • 25
    • 23644445334 scopus 로고    scopus 로고
    • Photo-cross-linking interacting proteins with a genetically encoded benzophenone
    • 16170867,.;: –;
    • Farrell IS, Toroney R, Hazen JL, Mehl RA, Chin JW, Photo-cross-linking interacting proteins with a genetically encoded benzophenone. Nat Methods. 2005;2: 377–;384. doi: 10.1038/nmeth0505-37716170867
    • (2005) Nat Methods , vol.2 , pp. 377-384
    • Farrell, I.S.1    Toroney, R.2    Hazen, J.L.3    Mehl, R.A.4    Chin, J.W.5
  • 29
    • 79955901001 scopus 로고    scopus 로고
    • Preserving the membrane barrier for small molecules during bacterial protein translocation
    • Park E, Rapoport TA, Preserving the membrane barrier for small molecules during bacterial protein translocation. Nature. Nature Publishing Group; 2011;473: 239–;242.
    • (2011) Nature. Nature Publishing Group , vol.473 , pp. 239-242
    • Park, E.1    Rapoport, T.A.2
  • 30
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • 15528446,.;: –;
    • Marlovits TC, Kubori T, Sukhan A, Thomas DR, Galán JE, Unger VM, Structural insights into the assembly of the type III secretion needle complex. Science. 2004;306: 1040–;1042. doi: 10.1126/science.110261015528446
    • (2004) Science , vol.306 , pp. 1040-1042
    • Marlovits, T.C.1    Kubori, T.2    Sukhan, A.3    Thomas, D.R.4    Galán, J.E.5    Unger, V.M.6
  • 31
    • 1842454268 scopus 로고    scopus 로고
    • Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB
    • 15060055,.;: –;
    • Van Arnam JS, McMurry JL, Kihara M, Macnab RM, Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB. J Bacteriol. 2004;186: 2495–;2498. doi: 10.1128/JB.186.8.2495-2498.200415060055
    • (2004) J Bacteriol , vol.186 , pp. 2495-2498
    • Van Arnam, J.S.1    McMurry, J.L.2    Kihara, M.3    Macnab, R.M.4
  • 32
    • 33745279057 scopus 로고    scopus 로고
    • Assembly of the inner rod determines needle length in the type III secretion injectisome
    • 16738660,.;: –;
    • Marlovits TC, Kubori T, Lara-Tejero M, Thomas D, Unger VM, Galán JE, Assembly of the inner rod determines needle length in the type III secretion injectisome. Nature. 2006;441: 637–;640. doi: 10.1038/nature0482216738660
    • (2006) Nature , vol.441 , pp. 637-640
    • Marlovits, T.C.1    Kubori, T.2    Lara-Tejero, M.3    Thomas, D.4    Unger, V.M.5    Galán, J.E.6
  • 33
    • 84892608956 scopus 로고    scopus 로고
    • The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system
    • 24379359,.;: –;
    • Lefebre MD, Lefebre MD, Galan JE, Galán JE, The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system. Proc Natl Acad Sci USA. 2014;111: 817–;822. doi: 10.1073/pnas.131969811124379359
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 817-822
    • Lefebre, M.D.1    Lefebre, M.D.2    Galan, J.E.3    Galán, J.E.4
  • 34
    • 0030983817 scopus 로고    scopus 로고
    • The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: putative components for flagellar assembly
    • 9324257,.;: –;
    • Ohnishi K, Fan F, Schoenhals GJ, Kihara M, Macnab RM, The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: putative components for flagellar assembly. J Bacteriol. 1997;179: 6092–;6099. 9324257
    • (1997) J Bacteriol , vol.179 , pp. 6092-6099
    • Ohnishi, K.1    Fan, F.2    Schoenhals, G.J.3    Kihara, M.4    Macnab, R.M.5
  • 35
    • 77954612287 scopus 로고    scopus 로고
    • Membrane topology of conserved components of the type III secretion system from the plant pathogen Xanthomonas campestris pv. vesicatoria
    • Berger C, Robin GP, Bonas U, Koebnik R, Membrane topology of conserved components of the type III secretion system from the plant pathogen Xanthomonas campestris pv. vesicatoria. Microbiology (Reading, Engl). 2010;156: 1963–;1974.
    • (2010) Microbiology (Reading, Engl) , vol.156 , pp. 1963-1974
    • Berger, C.1    Robin, G.P.2    Bonas, U.3    Koebnik, R.4
  • 36
    • 0028124264 scopus 로고
    • YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion
    • 8045883,.;: –;
    • Allaoui A, Woestyn S, Sluiters C, Cornelis GR, YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion. J Bacteriol. 1994;176: 4534–;4542. 8045883
    • (1994) J Bacteriol , vol.176 , pp. 4534-4542
    • Allaoui, A.1    Woestyn, S.2    Sluiters, C.3    Cornelis, G.R.4
  • 37
    • 0019407618 scopus 로고
    • Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines
    • 7015147,.;: –;
    • Hoiseth SK, Stocker BA, Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines. Nature. 1981;291: 238–;239. 7015147
    • (1981) Nature , vol.291 , pp. 238-239
    • Hoiseth, S.K.1    Stocker, B.A.2
  • 38
    • 33746486656 scopus 로고    scopus 로고
    • Oligomeric states of proteins determined by size-exclusion chromatography coupled with light scattering, absorbance, and refractive index detectors
    • Folta-Stogniew E, Oligomeric states of proteins determined by size-exclusion chromatography coupled with light scattering, absorbance, and refractive index detectors. Methods Mol Biol. New Jersey: Humana Press; 2006;328: 97–;112.
    • (2006) Methods Mol Biol. New Jersey: Humana Press , vol.328 , pp. 97-112
    • Folta-Stogniew, E.1
  • 39
    • 33846811132 scopus 로고    scopus 로고
    • An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-ToF instrument
    • Pringle SD, Giles K, Wildgoose JL, Williams JP, Slade SE, Thalassinos K, et al. An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-ToF instrument. International Journal of Mass Spectrometry. 2007;261: 1–;12.
    • (2007) International Journal of Mass Spectrometry , vol.261 , pp. 1-12
    • Pringle, S.D.1    Giles, K.2    Wildgoose, J.L.3    Williams, J.P.4    Slade, S.E.5    Thalassinos, K.6
  • 40
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • 17406634,.;: –;
    • Hernández H, Robinson CV, Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat Protoc. 2007;2: 715–;726. doi: 10.1038/nprot.2007.7317406634
    • (2007) Nat Protoc , vol.2 , pp. 715-726
    • Hernández, H.1    Robinson, C.V.2
  • 42
    • 37249037182 scopus 로고    scopus 로고
    • Molecular code for transmembrane-helix recognition by the Sec61 translocon
    • 18075582,..;: –;
    • Hessa T, Meindl-Beinker NM, Bernsel A, Kim H, Sato Y, Lerch-Bader M, et al. Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature. 2007;450: 1026–;1030. doi: 10.1038/nature0638718075582
    • (2007) Nature , vol.450 , pp. 1026-1030
    • Hessa, T.1    Meindl-Beinker, N.M.2    Bernsel, A.3    Kim, H.4    Sato, Y.5    Lerch-Bader, M.6
  • 43
    • 84897873840 scopus 로고    scopus 로고
    • Protter: interactive protein feature visualization and integration with experimental proteomic data
    • Omasits U, Ahrens CH, Müller S, Wollscheid B, Protter: interactive protein feature visualization and integration with experimental proteomic data. Bioinformatics. Oxford University Press; 2014;30: 884–;886.
    • (2014) Bioinformatics. Oxford University Press , vol.30 , pp. 884-886
    • Omasits, U.1    Ahrens, C.H.2    Müller, S.3    Wollscheid, B.4
  • 45
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber J, Mann M, Ishihama Y, Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc. Nature Publishing Group; 2007;2: 1896–;1906.
    • (2007) Nat Protoc. Nature Publishing Group , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 47
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M, MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol. Nature Publishing Group; 2008;26: 1367–;1372.
    • (2008) Nat Biotechnol. Nature Publishing Group , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 52
    • 84884603324 scopus 로고    scopus 로고
    • Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich era
    • Kamisetty H, Ovchinnikov S, Baker D, Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich era. Proc Natl Acad Sci USA. National Acad Sciences; 2013;110: 15674–;15679.
    • (2013) Proc Natl Acad Sci USA. National Acad Sciences , vol.110 , pp. 15674-15679
    • Kamisetty, H.1    Ovchinnikov, S.2    Baker, D.3
  • 54
    • 84925267288 scopus 로고    scopus 로고
    • UniRef clusters: a comprehensive and scalable alternative for improving sequence similarity searches
    • Suzek BE, Wang Y, Huang H, McGarvey PB, Wu CH, UniProt ConsortiumUniRef clusters: a comprehensive and scalable alternative for improving sequence similarity searches. Bioinformatics. Oxford University Press; 2015;31: 926–;932.
    • (2015) Bioinformatics. Oxford University Press , vol.31 , pp. 926-932
    • Suzek, B.E.1    Wang, Y.2    Huang, H.3    McGarvey, P.B.4    Wu, C.H.5
  • 55
    • 34247481878 scopus 로고    scopus 로고
    • IPython: A system for interactive scientific computing
    • Perez F, Granger BE, IPython: A system for interactive scientific computing. Comput Sci Eng. 2007;9: 21–;29.
    • (2007) Comput Sci Eng , vol.9 , pp. 21-29
    • Perez, F.1    Granger, B.E.2
  • 56
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: the new Leginon system
    • 15890530,..;: –;
    • Suloway C, Pulokas J, Fellmann D, Cheng A, Guerra F, Quispe J, et al. Automated molecular microscopy: the new Leginon system. J Struct Biol. 2005;151: 41–;60. doi: 10.1016/j.jsb.2005.03.01015890530
    • (2005) J Struct Biol , vol.151 , pp. 41-60
    • Suloway, C.1    Pulokas, J.2    Fellmann, D.3    Cheng, A.4    Guerra, F.5    Quispe, J.6
  • 57
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron microscopy
    • 16859925,..;: –;
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, et al. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol. 2007;157: 38–;46. doi: 10.1016/j.jsb.2006.05.00916859925
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6


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