메뉴 건너뛰기




Volumn 107, Issue 25, 2010, Pages 11295-11300

FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system

Author keywords

Chaperone; Flagella biosynthesis; Motility; Protein transport

Indexed keywords

ADAPTOR PROTEIN; FLAGELLIN; PROTEIN FLHA; PROTEIN FLID; PROTEIN FLIJ; PROTEIN FLIT; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CHAPERONE; FLAD PROTEIN, BACTERIA; FLHA PROTEIN, BACTERIA; FLIJ PROTEIN, BACTERIA; FLIT PROTEIN, BACTERIA; MEMBRANE PROTEIN;

EID: 77954920256     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1001383107     Document Type: Article
Times cited : (138)

References (41)
  • 1
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab RM (2003) How bacteria assemble flagella. Annu Rev Microbiol 57:77-100.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 2
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance FF, Hughes KT (2008) Coordinating assembly of a bacterial macromolecular machine. Nat Rev Microbiol 6:455-465.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 455-465
    • Chevance, F.F.1    Hughes, K.T.2
  • 3
    • 33645844248 scopus 로고    scopus 로고
    • Regulation of flagella
    • McCarter LL (2006) Regulation of flagella. Curr Opin Microbiol 9:180-186.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 180-186
    • McCarter, L.L.1
  • 4
    • 0030741128 scopus 로고    scopus 로고
    • Roles for motility in bacterial-host interactions
    • Ottemann KM, Miller JF (1997) Roles for motility in bacterial-host interactions. Mol Microbiol 24:1109-1117.
    • (1997) Mol Microbiol , vol.24 , pp. 1109-1117
    • Ottemann, K.M.1    Miller, J.F.2
  • 6
    • 0022429540 scopus 로고
    • "Cap" on the tip of Salmonella flagella
    • Ikeda T, Asakura S, Kamiya R (1985) "Cap" on the tip of Salmonella flagella. J Mol Biol 184:735-737.
    • (1985) J Mol Biol , vol.184 , pp. 735-737
    • Ikeda, T.1    Asakura, S.2    Kamiya, R.3
  • 7
    • 2642559479 scopus 로고    scopus 로고
    • Self-assembly and type III protein export of the bacterial flagellum
    • Minamino T, Namba K (2004) Self-assembly and type III protein export of the bacterial flagellum. J Mol Microb Biotech 7:5-17.
    • (2004) J Mol Microb Biotech , vol.7 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 8
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino T, Namba K (2008) Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature 451:485-488.
    • (2008) Nature , vol.451 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 10
    • 38849131977 scopus 로고    scopus 로고
    • Energizing type III secretion machines: What is the fuel?
    • Galan JE (2008) Energizing type III secretion machines: What is the fuel? Nat Struct Mol Biol 15:127-128.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 127-128
    • Galan, J.E.1
  • 11
    • 0035957518 scopus 로고    scopus 로고
    • Flagellin polymerisation control by a cytosolic export chaperone
    • Auvray F, Thomas J, Fraser GM, Hughes C (2001) Flagellin polymerisation control by a cytosolic export chaperone. J Mol Biol 308:221-229.
    • (2001) J Mol Biol , vol.308 , pp. 221-229
    • Auvray, F.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 12
    • 0035133472 scopus 로고    scopus 로고
    • Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT
    • Bennett JC, Thomas J, Fraser GM, Hughes C (2001) Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT. Mol Microbiol 39:781-791.
    • (2001) Mol Microbiol , vol.39 , pp. 781-791
    • Bennett, J.C.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 13
    • 0032906245 scopus 로고    scopus 로고
    • Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly
    • Fraser GM, Bennett JC, Hughes C (1999) Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Mol Microbiol 32:569-580.
    • (1999) Mol Microbiol , vol.32 , pp. 569-580
    • Fraser, G.M.1    Bennett, J.C.2    Hughes, C.3
  • 14
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
    • Thomas J, Stafford GP, Hughes C (2004) Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export. Proc Natl Acad Sci USA 101:3945-3950.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 15
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda Y, Galan JE (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    Galan, J.E.2
  • 16
    • 0344825097 scopus 로고    scopus 로고
    • Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli
    • Gauthier A, Finlay BB (2003) Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli. J Bacteriol 185:6747-6755.
    • (2003) J Bacteriol , vol.185 , pp. 6747-6755
    • Gauthier, A.1    Finlay, B.B.2
  • 17
    • 8844249277 scopus 로고    scopus 로고
    • Type III flagellar protein export and flagellar assembly
    • Macnab RM (2004) Type III flagellar protein export and flagellar assembly. Biochim Biophys Acta 1694:207-217.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 207-217
    • Macnab, R.M.1
  • 18
    • 41949132625 scopus 로고    scopus 로고
    • Piecing together the type III injectisome of bacterial pathogens
    • Moraes TF, Spreter T, Strynadka NC (2008) Piecing together the type III injectisome of bacterial pathogens. Curr Opin Struct Biol 18:258-266.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 258-266
    • Moraes, T.F.1    Spreter, T.2    Strynadka, N.C.3
  • 19
    • 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
    • Fan F, Ohnishi K, Francis NR, Macnab RM (1997) 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 26:1035-1046.
    • (1997) Mol Microbiol , vol.26 , pp. 1035-1046
    • Fan, F.1    Ohnishi, K.2    Francis, N.R.3    Macnab, R.M.4
  • 20
    • 0033059596 scopus 로고    scopus 로고
    • Components of the Salmonella flagellar export apparatus and classification of export substrates
    • Minamino T, Macnab RM (1999) Components of the Salmonella flagellar export apparatus and classification of export substrates. J Bacteriol 181:1388-1394.
    • (1999) J Bacteriol , vol.181 , pp. 1388-1394
    • Minamino, T.1    Macnab, R.M.2
  • 21
    • 0029730706 scopus 로고    scopus 로고
    • Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium
    • Fan F, Macnab RM (1996) Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium. J Biol Chem 271:31981-31988.
    • (1996) J Biol Chem , vol.271 , pp. 31981-31988
    • Fan, F.1    Macnab, R.M.2
  • 22
    • 0033779545 scopus 로고    scopus 로고
    • FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity
    • Minamino T, MacNab RM (2000) FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity. Mol Microbiol 37:1494-1503.
    • (2000) Mol Microbiol , vol.37 , pp. 1494-1503
    • Minamino, T.1    MacNab, R.M.2
  • 23
    • 35748929649 scopus 로고    scopus 로고
    • Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway
    • Stafford GP, et al. (2007) Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway. J Mol Biol 374:877-882.
    • (2007) J Mol Biol , vol.374 , pp. 877-882
    • Stafford, G.P.1
  • 25
    • 62549099973 scopus 로고    scopus 로고
    • Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
    • Evans LD, Hughes C (2009) Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO. FEMS Microbiol Lett 293:292-297.
    • (2009) FEMS Microbiol Lett , vol.293 , pp. 292-297
    • Evans, L.D.1    Hughes, C.2
  • 26
    • 0035110827 scopus 로고    scopus 로고
    • Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus
    • Kihara M, Minamino T, Yamaguchi S, Macnab RM (2001) Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus. J Bacteriol 183:1655-1662.
    • (2001) J Bacteriol , vol.183 , pp. 1655-1662
    • Kihara, M.1    Minamino, T.2    Yamaguchi, S.3    Macnab, R.M.4
  • 27
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck CJ (1998) Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62:379-433.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 28
    • 7744223028 scopus 로고    scopus 로고
    • Analysis of the cytoplasmic domains of Salmonella FlhA and interactions with components of the flagellar export machinery
    • McMurry JL, Van Arnam JS, Kihara M, Macnab RM (2004) Analysis of the cytoplasmic domains of Salmonella FlhA and interactions with components of the flagellar export machinery. J Bacteriol 186:7586-7592.
    • (2004) J Bacteriol , vol.186 , pp. 7586-7592
    • McMurry, J.L.1    Van Arnam, J.S.2    Kihara, M.3    Macnab, R.M.4
  • 29
    • 0027469764 scopus 로고
    • Bacillus subtilis FlhA: A flagellar protein related to a new family of signal-transducing receptors
    • Carpenter PB, Ordal GW (1993) Bacillus subtilis FlhA: A flagellar protein related to a new family of signal-transducing receptors. Mol Microbiol 7:735-743.
    • (1993) Mol Microbiol , vol.7 , pp. 735-743
    • Carpenter, P.B.1    Ordal, G.W.2
  • 30
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino T, MacNab RM (2000) Interactions among components of the Salmonella flagellar export apparatus and its substrates. Mol Microbiol 35:1052-1064.
    • (2000) Mol Microbiol , vol.35 , pp. 1052-1064
    • Minamino, T.1    MacNab, R.M.2
  • 31
    • 0036889293 scopus 로고    scopus 로고
    • Requirement of flhA for swarming differentiation, flagellin export, and secretion of virulence-associated proteins in Bacillus thuringiensis
    • Ghelardi E, et al. (2002) Requirement of flhA for swarming differentiation, flagellin export, and secretion of virulence-associated proteins in Bacillus thuringiensis. J Bacteriol 184:6424-6433.
    • (2002) J Bacteriol , vol.184 , pp. 6424-6433
    • Ghelardi, E.1
  • 32
    • 0041836042 scopus 로고    scopus 로고
    • Interactions of FliJ with the Salmonella type III flagellar export apparatus
    • Fraser GM, Gonzalez-Pedrajo B, Tame JR, Macnab RM (2003) Interactions of FliJ with the Salmonella type III flagellar export apparatus. J Bacteriol 185:5546-5554.
    • (2003) J Bacteriol , vol.185 , pp. 5546-5554
    • Fraser, G.M.1    Gonzalez-Pedrajo, B.2    Tame, J.R.3    Macnab, R.M.4
  • 33
    • 77949662091 scopus 로고    scopus 로고
    • Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export
    • in press
    • Minamino T, et al. Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export. J Bacteriol, in press.
    • J Bacteriol
    • Minamino, T.1
  • 34
    • 67749143715 scopus 로고    scopus 로고
    • The Helicobacter pylori anti-sigma factor FlgM is predominantly cytoplasmic and cooperates with the flagellar basal body protein FlhA
    • Rust M, et al. (2009) The Helicobacter pylori anti-sigma factor FlgM is predominantly cytoplasmic and cooperates with the flagellar basal body protein FlhA. J Bacteriol 191:4824-4834.
    • (2009) J Bacteriol , vol.191 , pp. 4824-4834
    • Rust, M.1
  • 35
    • 0141618445 scopus 로고    scopus 로고
    • Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion
    • Evdokimov AG, et al. (2003) Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion. Nat Struct Biol 10:789-793.
    • (2003) Nat Struct Biol , vol.10 , pp. 789-793
    • Evdokimov, A.G.1
  • 36
    • 0037469629 scopus 로고    scopus 로고
    • The FliS chaperone selectively binds the disordered flagellin C-terminal D0 domain central to polymerisation
    • Ozin AJ, Claret L, Auvray F, Hughes C (2003) The FliS chaperone selectively binds the disordered flagellin C-terminal D0 domain central to polymerisation. FEMS Microbiol Lett 219:219-224.
    • (2003) FEMS Microbiol Lett , vol.219 , pp. 219-224
    • Ozin, A.J.1    Claret, L.2    Auvray, F.3    Hughes, C.4
  • 37
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C (1995) Dali: A network tool for protein structure comparison. Trends Biochem Sci 20:478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 38
    • 4644346442 scopus 로고    scopus 로고
    • Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella
    • Saijo-Hamano Y, Minamino T, Macnab RM, Namba K (2004) Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella. J Mol Biol 343:457-466.
    • (2004) J Mol Biol , vol.343 , pp. 457-466
    • Saijo-Hamano, Y.1    Minamino, T.2    Macnab, R.M.3    Namba, K.4
  • 39
    • 0036041918 scopus 로고    scopus 로고
    • Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway
    • Gonzalez-Pedrajo B, Fraser GM, Minamino T, Macnab RM (2002) Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway. Mol Microbiol 45:967-982.
    • (2002) Mol Microbiol , vol.45 , pp. 967-982
    • Gonzalez-Pedrajo, B.1    Fraser, G.M.2    Minamino, T.3    Macnab, R.M.4
  • 40
    • 0021923816 scopus 로고
    • Locations of hook-associated proteins in flagellar structures of Salmonella typhimurium
    • Homma M, Iino T (1985) Locations of hook-associated proteins in flagellar structures of Salmonella typhimurium. J Bacteriol 162:183-189.
    • (1985) J Bacteriol , vol.162 , pp. 183-189
    • Homma, M.1    Iino, T.2
  • 41
    • 0034671834 scopus 로고    scopus 로고
    • The bacterial flagellar cap as the rotary promoter of flagellin self-assembly
    • Yonekura K, et al. (2000) The bacterial flagellar cap as the rotary promoter of flagellin self-assembly. Science 290:2148-2152.
    • (2000) Science , vol.290 , pp. 2148-2152
    • Yonekura, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.