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Volumn 23, Issue 5, 2015, Pages 296-300

Fueling type III secretion

Author keywords

ATPase; Flagellum; Needle complex; Proton motive force; T3SS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; TYPE III SECRETION SYSTEM;

EID: 84937639127     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2015.01.012     Document Type: Review
Times cited : (50)

References (40)
  • 1
    • 84907563228 scopus 로고    scopus 로고
    • Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells
    • Galan J.E., et al. Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells. Annu. Rev. Microbiol. 2014, 68:415-438.
    • (2014) Annu. Rev. Microbiol. , vol.68 , pp. 415-438
    • Galan, J.E.1
  • 2
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda Y., Galan J.E. Chaperone release and unfolding of substrates in type III secretion. Nature 2005, 437:911-915.
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 3
    • 84923284551 scopus 로고    scopus 로고
    • Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus
    • Bai F., et al. Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus. Sci. Rep. 2014, 4:6528.
    • (2014) Sci. Rep. , vol.4 , pp. 6528
    • Bai, F.1
  • 4
    • 77954920256 scopus 로고    scopus 로고
    • FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system
    • Bange G., et al. FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:11295-11300.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11295-11300
    • Bange, G.1
  • 5
    • 84890123592 scopus 로고    scopus 로고
    • Interactions of bacterial flagellar chaperone-substrate complexes with FlhA contribute to co-ordinating assembly of the flagellar filament
    • Kinoshita M., et al. Interactions of bacterial flagellar chaperone-substrate complexes with FlhA contribute to co-ordinating assembly of the flagellar filament. Mol. Microbiol. 2013, 90:1249-1261.
    • (2013) Mol. Microbiol. , vol.90 , pp. 1249-1261
    • Kinoshita, M.1
  • 6
    • 79952280754 scopus 로고    scopus 로고
    • A sorting platform determines the order of protein secretion in bacterial type III systems
    • Lara-Tejero M., et al. A sorting platform determines the order of protein secretion in bacterial type III systems. Science 2011, 331:1188-1191.
    • (2011) Science , vol.331 , pp. 1188-1191
    • Lara-Tejero, M.1
  • 7
    • 84872007514 scopus 로고    scopus 로고
    • Architecture of the major component of the type III secretion system export apparatus
    • Abrusci P., et al. Architecture of the major component of the type III secretion system export apparatus. Nat. Struct. Mol. Biol. 2013, 20:99-104.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 99-104
    • Abrusci, P.1
  • 8
    • 84890436185 scopus 로고    scopus 로고
    • A chain mechanism for flagellum growth
    • Evans L.D., et al. A chain mechanism for flagellum growth. Nature 2013, 504:287-290.
    • (2013) Nature , vol.504 , pp. 287-290
    • Evans, L.D.1
  • 9
    • 33646489548 scopus 로고    scopus 로고
    • Type III secretion: what's in a name?
    • Desvaux M., et al. Type III secretion: what's in a name?. Trends Microbiol. 2006, 14:157-160.
    • (2006) Trends Microbiol. , vol.14 , pp. 157-160
    • Desvaux, M.1
  • 10
    • 84889777894 scopus 로고    scopus 로고
    • Common and distinct structural features of Salmonella injectisome and flagellar basal body
    • Kawamoto A., et al. Common and distinct structural features of Salmonella injectisome and flagellar basal body. Sci. Rep. 2013, 3:3369.
    • (2013) Sci. Rep. , vol.3 , pp. 3369
    • Kawamoto, A.1
  • 11
    • 43449122166 scopus 로고    scopus 로고
    • The type III secretion system tip complex and translocon
    • Mueller C.A., et al. The type III secretion system tip complex and translocon. Mol. Microbiol. 2008, 68:1085-1095.
    • (2008) Mol. Microbiol. , vol.68 , pp. 1085-1095
    • Mueller, C.A.1
  • 12
    • 84893742076 scopus 로고    scopus 로고
    • Structure of a pathogenic type 3 secretion system in action
    • Radics J., et al. Structure of a pathogenic type 3 secretion system in action. Nat. Struct. Mol. Biol. 2014, 21:82-87.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 82-87
    • Radics, J.1
  • 13
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino T., Namba K. Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature 2008, 451:485-488.
    • (2008) Nature , vol.451 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 14
    • 38549088345 scopus 로고    scopus 로고
    • Energy source of flagellar type III secretion
    • Paul K., et al. Energy source of flagellar type III secretion. Nature 2008, 451:489-492.
    • (2008) Nature , vol.451 , pp. 489-492
    • Paul, K.1
  • 15
    • 76149140076 scopus 로고    scopus 로고
    • A repulsive electrostatic mechanism for protein export through the type III secretion apparatus
    • Rathinavelan T., et al. A repulsive electrostatic mechanism for protein export through the type III secretion apparatus. Biophys. J. 2010, 98:452-461.
    • (2010) Biophys. J. , vol.98 , pp. 452-461
    • Rathinavelan, T.1
  • 16
    • 0035423161 scopus 로고    scopus 로고
    • Targeting exported substrates to the Yersinia TTSS: different functions for different signals?
    • Lloyd S.A., et al. Targeting exported substrates to the Yersinia TTSS: different functions for different signals?. Trends Microbiol. 2001, 9:367-371.
    • (2001) Trends Microbiol. , vol.9 , pp. 367-371
    • Lloyd, S.A.1
  • 17
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot C., et al. The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 2003, 6:7-14.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1
  • 18
    • 84906544286 scopus 로고    scopus 로고
    • Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo
    • Allison S.E., et al. Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo. J. Biol. Chem. 2014, 289:23734-23744.
    • (2014) J. Biol. Chem. , vol.289 , pp. 23734-23744
    • Allison, S.E.1
  • 19
    • 33846941536 scopus 로고    scopus 로고
    • Structural analysis of a prototypical ATPase from the type III secretion system
    • Zarivach R., et al. Structural analysis of a prototypical ATPase from the type III secretion system. Nat. Struct. Mol. Biol. 2007, 14:131-137.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 131-137
    • Zarivach, R.1
  • 20
    • 8844251486 scopus 로고    scopus 로고
    • Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
    • Weibezahn J., et al. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 2004, 119:653-665.
    • (2004) Cell , vol.119 , pp. 653-665
    • Weibezahn, J.1
  • 21
    • 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., et al. Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB. Infect. Immun. 2004, 72:4004-4009.
    • (2004) Infect. Immun. , vol.72 , pp. 4004-4009
    • Wilharm, G.1
  • 22
    • 84900513743 scopus 로고    scopus 로고
    • Control of type III secretion activity and substrate specificity by the cytoplasmic regulator PcrG
    • Lee P.C., et al. Control of type III secretion activity and substrate specificity by the cytoplasmic regulator PcrG. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:E2027-E2036.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. E2027-E2036
    • Lee, P.C.1
  • 23
    • 1842506700 scopus 로고    scopus 로고
    • Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains
    • Akeda Y., Galan J.E. Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains. J. Bacteriol. 2004, 186:2402-2412.
    • (2004) J. Bacteriol. , vol.186 , pp. 2402-2412
    • Akeda, Y.1    Galan, J.E.2
  • 24
    • 84881044066 scopus 로고    scopus 로고
    • In situ structural analysis of the Yersinia enterocolitica injectisome
    • Kudryashev M., et al. In situ structural analysis of the Yersinia enterocolitica injectisome. eLife 2013, 2:e00792.
    • (2013) eLife , vol.2 , pp. e00792
    • Kudryashev, M.1
  • 25
    • 80053415915 scopus 로고    scopus 로고
    • An energy transduction mechanism used in bacterial flagellar type III protein export
    • Minamino T., et al. An energy transduction mechanism used in bacterial flagellar type III protein export. Nat. Commun. 2011, 2:475.
    • (2011) Nat. Commun. , vol.2 , pp. 475
    • Minamino, T.1
  • 26
    • 79960463317 scopus 로고    scopus 로고
    • Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA
    • Hara N., et al. Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA. PLoS ONE 2011, 6:e22417.
    • (2011) PLoS ONE , vol.6 , pp. e22417
    • Hara, N.1
  • 27
    • 84873051807 scopus 로고    scopus 로고
    • Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus
    • Ibuki T., et al. Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus. J. Bacteriol. 2013, 195:466-473.
    • (2013) J. Bacteriol. , vol.195 , pp. 466-473
    • Ibuki, T.1
  • 28
    • 0015518441 scopus 로고
    • Reconstruction of Salmonella flagella attached to cell bodies
    • Iino T., et al. Reconstruction of Salmonella flagella attached to cell bodies. Nat. New Biol. 1972, 237:238-240.
    • (1972) Nat. New Biol. , vol.237 , pp. 238-240
    • Iino, T.1
  • 29
    • 0029039662 scopus 로고
    • The structure of the R-type straight flagellar filament of Salmonella at 9Å resolution by electron cryomicroscopy
    • Mimori Y., et al. The structure of the R-type straight flagellar filament of Salmonella at 9Å resolution by electron cryomicroscopy. J. Mol. Biol. 1995, 249:69-87.
    • (1995) J. Mol. Biol. , vol.249 , pp. 69-87
    • Mimori, Y.1
  • 30
    • 0029042213 scopus 로고
    • Structure of bacterial flagellar filaments at 11Å resolution: packing of the alpha-helices
    • Morgan D.G., et al. Structure of bacterial flagellar filaments at 11Å resolution: packing of the alpha-helices. J. Mol. Biol. 1995, 249:88-110.
    • (1995) J. Mol. Biol. , vol.249 , pp. 88-110
    • Morgan, D.G.1
  • 31
    • 84879820469 scopus 로고    scopus 로고
    • Single-file diffusion of flagellin in flagellar filaments
    • Stern A.S., Berg H.C. Single-file diffusion of flagellin in flagellar filaments. Biophys. J. 2013, 105:182-184.
    • (2013) Biophys. J. , vol.105 , pp. 182-184
    • Stern, A.S.1    Berg, H.C.2
  • 32
    • 38849131977 scopus 로고    scopus 로고
    • Energizing type III secretion machines: what is the fuel?
    • Galan J.E. Energizing type III secretion machines: what is the fuel?. Nat. Struct. Mol. Biol. 2008, 15:127-128.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 127-128
    • Galan, J.E.1
  • 33
    • 84861388575 scopus 로고    scopus 로고
    • Growth of flagellar filaments of Escherichia coli is independent of filament length
    • Turner L., et al. Growth of flagellar filaments of Escherichia coli is independent of filament length. J. Bacteriol. 2012, 194:2437-2442.
    • (2012) J. Bacteriol. , vol.194 , pp. 2437-2442
    • Turner, L.1
  • 34
    • 0014515268 scopus 로고
    • Polarity of flagellar growth in Salmonella
    • Iino T. Polarity of flagellar growth in Salmonella. J. Gen. Microbiol. 1969, 56:227-239.
    • (1969) J. Gen. Microbiol. , vol.56 , pp. 227-239
    • Iino, T.1
  • 35
    • 0031735650 scopus 로고    scopus 로고
    • Bacterial flagellation and cell division
    • Aizawa S.I., Kubori T. Bacterial flagellation and cell division. Genes Cells 1998, 3:625-634.
    • (1998) Genes Cells , vol.3 , pp. 625-634
    • Aizawa, S.I.1    Kubori, T.2
  • 36
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson D.M., Schneewind O. A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 1997, 278:1140-1143.
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 37
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory M.P., Cornelis G.R. Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol. Microbiol. 1994, 14:583-594.
    • (1994) Mol. Microbiol. , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 38
    • 3843065509 scopus 로고    scopus 로고
    • Identification of the secretion and translocation domain of the enteropathogenic and enterohemorrhagic Escherichia coli effector Cif, using TEM-1 beta-lactamase as a new fluorescence-based reporter
    • Charpentier X., Oswald E. Identification of the secretion and translocation domain of the enteropathogenic and enterohemorrhagic Escherichia coli effector Cif, using TEM-1 beta-lactamase as a new fluorescence-based reporter. J. Bacteriol. 2004, 186:5486-5495.
    • (2004) J. Bacteriol. , vol.186 , pp. 5486-5495
    • Charpentier, X.1    Oswald, E.2
  • 39
    • 84863465427 scopus 로고    scopus 로고
    • Selective purification of recombinant neuroactive peptides using the flagellar type III secretion system
    • e00115-12.
    • Singer H.M., et al. Selective purification of recombinant neuroactive peptides using the flagellar type III secretion system. MBio 2012, 3:e00115-12.
    • (2012) MBio , vol.3
    • Singer, H.M.1
  • 40
    • 84919375565 scopus 로고    scopus 로고
    • High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy
    • Demers J.P., et al. High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy. Nat. Commun. 2014, 5:4976.
    • (2014) Nat. Commun. , vol.5 , pp. 4976
    • Demers, J.P.1


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