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Volumn 6, Issue 9, 2010, Pages

FliO regulation of FliP in the formation of the Salmonella enterica flagellum

Author keywords

[No Author keywords available]

Indexed keywords

FLICE INHIBITORY PROTEIN; FLIO PROTEIN; LEUCINE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 78049427928     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1001143     Document Type: Article
Times cited : (32)

References (48)
  • 1
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: Insights into their function from structural similarities
    • Blocker A, Komoriya K, Aizawa S-I (2003) Type III secretion systems and bacterial flagella: Insights into their function from structural similarities. Proc Natl Acad Sci U S A 100: 3027-3030.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3027-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.-I.3
  • 2
    • 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
  • 3
    • 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
  • 4
    • 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
  • 5
    • 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
  • 6
    • 1842454268 scopus 로고    scopus 로고
    • Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB
    • Van Arnam JS, McMurry JL, Kihara M, Macnab RM (2004) Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB. J Bacteriol 186: 2495-2498.
    • (2004) J Bacteriol , vol.186 , pp. 2495-2498
    • Van Arnam, J.S.1    McMurry, J.L.2    Kihara, M.3    Macnab, R.M.4
  • 7
    • 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
  • 8
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance FFV, 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.V.1    Hughes, K.T.2
  • 9
    • 58149347646 scopus 로고    scopus 로고
    • Mechanisms of type III protein export for bacterial flagellar assembly
    • Minamino T, Imada K, Namba K (2008) Mechanisms of type III protein export for bacterial flagellar assembly. Mol BioSyst 4: 1105-1115.
    • (2008) Mol BioSyst , vol.4 , pp. 1105-1115
    • Minamino, T.1    Imada, K.2    Namba, K.3
  • 10
    • 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
  • 12
    • 77950244006 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export
    • Saijo-Hamano Y, Imada K, Minamino T, Kihara M, Shimada M, et al. (2010) Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export. Mol Microbiol 76: 260-268.
    • (2010) Mol Microbiol , vol.76 , pp. 260-268
    • Saijo-Hamano, Y.1    Imada, K.2    Minamino, T.3    Kihara, M.4    Shimada, M.5
  • 13
    • 77954239967 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori
    • Moore SA, Jia Y (2010) Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori. J Biol Chem 285: 21060-21069.
    • (2010) J Biol Chem , vol.285 , pp. 21060-21069
    • Moore, S.A.1    Jia, Y.2
  • 14
    • 77954224937 scopus 로고    scopus 로고
    • Crystal structure of the Cterminal domain of the Salmonella type III secretion system export apparatus protein InvA
    • Worrall LJ, Vuckovic M, Strynadka NC (2010) Crystal structure of the Cterminal domain of the Salmonella type III secretion system export apparatus protein InvA. Protein Sci 19: 1091-1096.
    • (2010) Protein Sci , vol.19 , pp. 1091-1096
    • Worrall, L.J.1    Vuckovic, M.2    Strynadka, N.C.3
  • 15
    • 43049127811 scopus 로고    scopus 로고
    • Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS
    • Zarivach R, Deng W, Vuckovic M, Felise HB, Nguyen HV, et al. (2008) Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS. Nature 453: 124-127.
    • (2008) Nature , vol.453 , pp. 124-127
    • Zarivach, R.1    Deng, W.2    Vuckovic, M.3    Felise, H.B.4    Nguyen, H.V.5
  • 16
    • 45149126804 scopus 로고    scopus 로고
    • Crystal structure of Spa40, the specificity switch for the Shigella flexneri type III secretion system
    • Deane JE, Graham SC, Mitchell EP, Flot D, Johnson S, et al. (2008) Crystal structure of Spa40, the specificity switch for the Shigella flexneri type III secretion system. Mol Microbiol 69: 267-276.
    • (2008) Mol Microbiol , vol.69 , pp. 267-276
    • Deane, J.E.1    Graham, S.C.2    Mitchell, E.P.3    Flot, D.4    Johnson, S.5
  • 17
    • 59949084690 scopus 로고    scopus 로고
    • Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion
    • Lountos GT, Austin BP, Nallamsetty S, Waugh DS (2009) Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion. Prot Sci 18: 467-474.
    • (2009) Prot Sci , vol.18 , pp. 467-474
    • Lountos, G.T.1    Austin, B.P.2    Nallamsetty, S.3    Waugh, D.S.4
  • 18
    • 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
  • 19
    • 0041836042 scopus 로고    scopus 로고
    • Interactions of FliJ with the Salmonella type III flagellar export apparatus
    • Fraser GM, González-Pedrajo B, Tame JRH, 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    González-Pedrajo, B.2    Tame, J.R.H.3    Macnab, R.M.4
  • 20
    • 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
  • 21
    • 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
  • 22
    • 77949662091 scopus 로고    scopus 로고
    • Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export
    • Minamino T, Shimada M, Okabe M, Saijo-Hamano Y, Imada K, et al. (2010) Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export. J Bacteriol 192: 1929-1936.
    • (2010) J Bacteriol , vol.192 , pp. 1929-1936
    • Minamino, T.1    Shimada, M.2    Okabe, M.3    Saijo-Hamano, Y.4    Imada, K.5
  • 23
    • 0032827183 scopus 로고    scopus 로고
    • FliK, the protein responsible for flagellar hook length control in Salmonella, is exported during hook assembly
    • Minamino T, González-Pedrajo B, Yamaguchi K, Aizawa S-I, Macnab RM (1999) FliK, the protein responsible for flagellar hook length control in Salmonella, is exported during hook assembly. Mol Microbiol 34: 295-304.
    • (1999) Mol Microbiol , vol.34 , pp. 295-304
    • Minamino, T.1    González-Pedrajo, B.2    Yamaguchi, K.3    Aizawa, S.-I.4    Macnab, R.M.5
  • 24
    • 0033900964 scopus 로고    scopus 로고
    • Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching
    • Minamino T, Macnab RM (2000) Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching. J Bacteriol 182: 4906-4914.
    • (2000) J Bacteriol , vol.182 , pp. 4906-4914
    • Minamino, T.1    Macnab, R.M.2
  • 25
    • 0038016732 scopus 로고    scopus 로고
    • Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB
    • Fraser GM, Hirano T, Ferris HU, Devgan LL, Kihara M, et al. (2003) Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB. Mol Microbiol 48: 1043-1057.
    • (2003) Mol Microbiol , vol.48 , pp. 1043-1057
    • Fraser, G.M.1    Hirano, T.2    Ferris, H.U.3    Devgan, L.L.4    Kihara, M.5
  • 26
    • 29244467975 scopus 로고    scopus 로고
    • FlhB regulates ordered export of flagellar components via autocleavage mechanism
    • Ferris HU, Furukawa Y, Minamino T, Kroetz MB, Kihara M, et al. (2005) FlhB regulates ordered export of flagellar components via autocleavage mechanism. J Biol Chem 280: 41236-41242.
    • (2005) J Biol Chem , vol.280 , pp. 41236-41242
    • Ferris, H.U.1    Furukawa, Y.2    Minamino, T.3    Kroetz, M.B.4    Kihara, M.5
  • 27
    • 33748465285 scopus 로고    scopus 로고
    • Two parts of the T3S4 domain of the hook-length control protein FliK are essential for the substrate specificity switching of the flagellar type III export apparatus
    • Minamino T, Ferris HU, Moriya N, Kihara M, Namba K (2006) Two parts of the T3S4 domain of the hook-length control protein FliK are essential for the substrate specificity switching of the flagellar type III export apparatus. J Mol Biol 362: 1148-1158.
    • (2006) J Mol Biol , vol.362 , pp. 1148-1158
    • Minamino, T.1    Ferris, H.U.2    Moriya, N.3    Kihara, M.4    Namba, K.5
  • 28
    • 33646202330 scopus 로고    scopus 로고
    • The type III flagellar export specificity switch is dependent on FliK ruler and a molecular clock
    • Moriya N, Minamino T, Hughes KT, Macnab RM, Namba K (2006) The type III flagellar export specificity switch is dependent on FliK ruler and a molecular clock. J Mol Biol 359: 466-477.
    • (2006) J Mol Biol , vol.359 , pp. 466-477
    • Moriya, N.1    Minamino, T.2    Hughes, K.T.3    Macnab, R.M.4    Namba, K.5
  • 29
    • 77349103262 scopus 로고    scopus 로고
    • The role of the FliK molecular ruler in hook-length control in Salmonella enterica
    • Erhardt M, Hirano T, Su Y, Paul K, Wee DH, et al. (2010) The role of the FliK molecular ruler in hook-length control in Salmonella enterica. Mol Micro 75: 1272-1284.
    • (2010) Mol Micro , vol.75 , pp. 1272-1284
    • Erhardt, M.1    Hirano, T.2    Su, Y.3    Paul, K.4    Wee, D.H.5
  • 30
    • 0024594008 scopus 로고
    • DNA sequence analysis, gene product identification, and localization of flagellar motor components of Escherichia coli
    • Malakooti J, Komeda Y, Matsumura P (1989) DNA sequence analysis, gene product identification, and localization of flagellar motor components of Escherichia coli. J Bacteriol 171: 2728-2734.
    • (1989) J Bacteriol , vol.171 , pp. 2728-2734
    • Malakooti, J.1    Komeda, Y.2    Matsumura, P.3
  • 31
    • 0028057604 scopus 로고
    • Molecular characterization, nucleotide sequence, and expression of the fliO, fliP, fliQ, and fliR genes of Escherichia coli
    • Malakooti J, Ely B, Matsumura P (1994) Molecular characterization, nucleotide sequence, and expression of the fliO, fliP, fliQ, and fliR genes of Escherichia coli. J Bacteriol 176: 189-197.
    • (1994) J Bacteriol , vol.176 , pp. 189-197
    • Malakooti, J.1    Ely, B.2    Matsumura, P.3
  • 32
    • 0030983817 scopus 로고    scopus 로고
    • The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: Putative components for flagellar assembly
    • Ohnishi K, Fan F, Schoenhals GJ, Kihara M, Macnab RM (1997) The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: putative components for flagellar assembly. J Bacteriol 179: 6092-6099.
    • (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
  • 33
    • 0032455442 scopus 로고    scopus 로고
    • Translation of the flagellar gene fliO of Salmonella typhimurium from putative tandem starts
    • Schoenhals GJ, Kihara M, Macnab RM (1998) Translation of the flagellar gene fliO of Salmonella typhimurium from putative tandem starts. J Bacteriol 180: 2936-2942.
    • (1998) J Bacteriol , vol.180 , pp. 2936-2942
    • Schoenhals, G.J.1    Kihara, M.2    Macnab, R.M.3
  • 34
    • 34249856320 scopus 로고    scopus 로고
    • Stepwise formation of the bacterial flagellar system
    • Liu R, Ochman H (2007) Stepwise formation of the bacterial flagellar system. Proc Natl Acad Sci U S A 104: 7116-7121.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7116-7121
    • Liu, R.1    Ochman, H.2
  • 35
    • 16244411638 scopus 로고    scopus 로고
    • Bacterial flagellar diversity in the post-genomic era
    • Pallen MJ, Penn CW, Chaudhuri RR (2005) Bacterial flagellar diversity in the post-genomic era. Trends Microbiol 13: 143-149.
    • (2005) Trends Microbiol , vol.13 , pp. 143-149
    • Pallen, M.J.1    Penn, C.W.2    Chaudhuri, R.R.3
  • 36
    • 37049184497 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil C, Beckwith J (1986) A genetic approach to analyzing membrane protein topology. Science 233: 1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 37
    • 0025052350 scopus 로고
    • Genetic analysis of membrane protein topology by a sandwich gene fusion approach
    • Ehrmann M, Boyd D, Beckwith J (1990) Genetic analysis of membrane protein topology by a sandwich gene fusion approach. Proc Natl Acad Sci U S A 87: 7574-7578.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7574-7578
    • Ehrmann, M.1    Boyd, D.2    Beckwith, J.3
  • 38
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd D, Traxler B, Beckwith J (1993) Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J Bacteriol 175: 553-556.
    • (1993) J Bacteriol , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 39
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • Feilmeier BJ, Iseminger G, Schroeder D, Webber H, Phillips GJ (2000) Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J Bacteriol 182: 4068-4076.
    • (2000) J Bacteriol , vol.182 , pp. 4068-4076
    • Feilmeier, B.J.1    Iseminger, G.2    Schroeder, D.3    Webber, H.4    Phillips, G.J.5
  • 40
    • 0037022563 scopus 로고    scopus 로고
    • Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson JS, Richardson DC (2002) Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A 99: 2754-2759.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 41
    • 0034618559 scopus 로고    scopus 로고
    • Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS
    • Shigenobu S, Watanabe H, Hattori M, Sakaki Y, Ishikawa H (2000) Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS. Nature 407: 81-86.
    • (2000) Nature , vol.407 , pp. 81-86
    • Shigenobu, S.1    Watanabe, H.2    Hattori, M.3    Sakaki, Y.4    Ishikawa, H.5
  • 42
    • 0024227425 scopus 로고
    • Flagellin parts acquiring a regular structure during polymerization are disposed on the molecule ends
    • Kostyukova AS, Pyatibratov MG, Filimonov VV, Federov OV (1988) Flagellin parts acquiring a regular structure during polymerization are disposed on the molecule ends. FEBS Lett 241: 141-144.
    • (1988) FEBS Lett , vol.241 , pp. 141-144
    • Kostyukova, A.S.1    Pyatibratov, M.G.2    Filimonov, V.V.3    Federov, O.V.4
  • 43
    • 0034950529 scopus 로고    scopus 로고
    • Folding properties of functional domains of tropomodulin
    • Kostyukova AS, Tiktopulo EI, Maéda Y (2001) Folding properties of functional domains of tropomodulin. Biophys J 81: 345-351.
    • (2001) Biophys J , vol.81 , pp. 345-351
    • Kostyukova, A.S.1    Tiktopulo, E.I.2    Maéda, Y.3
  • 44
    • 0030447840 scopus 로고    scopus 로고
    • Deletion analysis of the FliM flagellar switch protein of Salmonella typhimurium
    • Toker AS, Kihara M, Macnab RM (1996) Deletion analysis of the FliM flagellar switch protein of Salmonella typhimurium. J Bacteriol 178: 7069-7079.
    • (1996) J Bacteriol , vol.178 , pp. 7069-7079
    • Toker, A.S.1    Kihara, M.2    Macnab, R.M.3
  • 45
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 46
    • 33847647657 scopus 로고    scopus 로고
    • L-Red genetic engineering in Salmonella enterica serovar Typhimurium
    • Karlinsey JE (2007) l-Red genetic engineering in Salmonella enterica serovar Typhimurium. Methods Enzymol 421: 199-209.
    • (2007) Methods Enzymol , vol.421 , pp. 199-209
    • Karlinsey, J.E.1
  • 47
    • 0033637740 scopus 로고    scopus 로고
    • Topological analysis and role of the transmembrane domain in polar targeting of PilS, a Pseudomonas aeruginosa sensor kinase
    • Ethier J, Boyd JM (2000) Topological analysis and role of the transmembrane domain in polar targeting of PilS, a Pseudomonas aeruginosa sensor kinase. Mol Microbiol 38: 891-903.
    • (2000) Mol Microbiol , vol.38 , pp. 891-903
    • Ethier, J.1    Boyd, J.M.2
  • 48
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C, Barber JD, Barton GJ (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36: W197-W201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3


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