메뉴 건너뛰기




Volumn 192, Issue 7, 2010, Pages 1929-1936

Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FLHA; FLHB; FLIH; FLII; FLIJ; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 77949662091     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01328-09     Document Type: Article
Times cited : (54)

References (32)
  • 1
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret, L., C. R. Susannah, M. Higgins, and C. Hughes. 2003. Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol. Microbiol. 48:1349-1355.
    • (2003) Mol. Microbiol , vol.48 , pp. 1349-1355
    • Claret, L.1    Susannah, C.R.2    Higgins, M.3    Hughes, C.4
  • 2
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner2
  • 4
    • 0029730706 scopus 로고    scopus 로고
    • Enzymatic characterization of FliI: An ATPase involved in flagellar assembly in Salmonella typhimurium
    • Fan, F., and R. M. Macnab. 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
  • 5
    • 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., K. Ohnishi, N. R. Francis, and R. M. Macnab. 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
  • 6
    • 0041836042 scopus 로고    scopus 로고
    • Interactions of FliJ with the Salmonella type III flagellar export apparatus
    • Fraser, G. M., B. González-Pedrajo, J. R. H. Tame, and R. M. Macnab. 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
  • 7
    • 67549133101 scopus 로고    scopus 로고
    • Hirano, T., S. Mizuno, S.-I. Aizawa, and K. T. Hughes. 2009. Mutations in Flk, FlgG, FlhA, and FlhE that affect the flagellar type III secretion specificity switch in Salmonella enterica. J. Bacteriol. 191:3938-3949.
    • Hirano, T., S. Mizuno, S.-I. Aizawa, and K. T. Hughes. 2009. Mutations in Flk, FlgG, FlhA, and FlhE that affect the flagellar type III secretion specificity switch in Salmonella enterica. J. Bacteriol. 191:3938-3949.
  • 9
    • 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., T. Minamino, S. Yamaguchi, and R. M. Macnab. 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
  • 10
    • 0021866614 scopus 로고
    • Refined genetic analysis of the region II che mutants in Salmonella typhimurium
    • Kutsukake, K., and T. Iino. 1985. Refined genetic analysis of the region II che mutants in Salmonella typhimurium. Mol. Gen. Genet. 199:406-409.
    • (1985) Mol. Gen. Genet , vol.199 , pp. 406-409
    • Kutsukake, K.1    Iino, T.2
  • 11
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R. M. 2003. How bacteria assemble flagella. Annu. Rev. Microbiol. 57:77-100.
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 12
    • 7744223028 scopus 로고    scopus 로고
    • Analysis of the cytoplasmic domains of Salmonella FlhA and interactions with components of the flagellar export machinery
    • McMurry, J. L., J. S. Van Arnam, M. Kihara, and R. M. Macnab. 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
  • 13
    • 0033924918 scopus 로고    scopus 로고
    • Role of FliJ in flagellar protein export in Salmonella
    • Minamino, T., R. Chu, S. Yamaguchi, and R. M. Macnab. 2000. Role of FliJ in flagellar protein export in Salmonella. J. Bacteriol. 182:4207-4215.
    • (2000) J. Bacteriol , vol.182 , pp. 4207-4215
    • Minamino, T.1    Chu, R.2    Yamaguchi, S.3    Macnab, R.M.4
  • 14
    • 0037701404 scopus 로고    scopus 로고
    • The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH
    • Minamino, T., B. González-Pedrajo, M. Kihara, K. Namba, and R. M. Macnab. 2003. The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH. J. Bacteriol. 185:3983-3988.
    • (2003) J. Bacteriol , vol.185 , pp. 3983-3988
    • Minamino, T.1    González-Pedrajo, B.2    Kihara, M.3    Namba, K.4    Macnab, R.M.5
  • 15
    • 0027997618 scopus 로고
    • Molecular characterization of the Salmonella typhimurium flhB operon and its protein products
    • Minamino, T., T. Iino, and K. Kutsukake. 1994. Molecular characterization of the Salmonella typhimurium flhB operon and its protein products. J. Bacteriol. 176:7630-7637.
    • (1994) J. Bacteriol , vol.176 , pp. 7630-7637
    • Minamino, T.1    Iino, T.2    Kutsukake, K.3
  • 16
    • 58149347646 scopus 로고    scopus 로고
    • Mechanisms of type III protein export for bacterial flagellar assembly
    • Minamino, T., K. Imada, and K. Namba. 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
  • 17
    • 33745276514 scopus 로고    scopus 로고
    • Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region
    • Minamino, T., K.-I. Kazetani, A. Tahara, H. Suzuki, Y. Furukawa, M. Kihara, and K. Namba. 2006. Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region. J. Mol. Biol. 360:510-519.
    • (2006) J. Mol. Biol , vol.360 , pp. 510-519
    • Minamino, T.1    Kazetani, K.-I.2    Tahara, A.3    Suzuki, H.4    Furukawa, Y.5    Kihara, M.6    Namba, K.7
  • 18
    • 0033059596 scopus 로고    scopus 로고
    • Components of the Salmonella flagellar export apparatus and classification of export substrates
    • Minamino, T., and R. M. Macnab. 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
  • 19
    • 0033900964 scopus 로고    scopus 로고
    • Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching
    • Minamino, T., and R. M. Macnab. 2000. Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching. J. Bacteriol. 182:4906-4919.
    • (2000) J. Bacteriol , vol.182 , pp. 4906-4919
    • Minamino, T.1    Macnab, R.M.2
  • 20
    • 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., and R. M. Macnab. 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
  • 21
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino, T., and R. M. Macnab. 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
  • 22
    • 2642559479 scopus 로고    scopus 로고
    • Self-assembly and type III protein export of the bacterial flagellum
    • Minamino, T., and K. Namba. 2004. Self-assembly and type III protein export of the bacterial flagellum. J. Mol. Microbiol. Biotechnol. 7:5-17.
    • (2004) J. Mol. Microbiol. Biotechnol , vol.7 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 23
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino, T., and K. Namba. 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
  • 24
    • 72049109167 scopus 로고    scopus 로고
    • Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus
    • Minamino, T., S. D. J. Yoshimura, Y. V. Morimoto, B. González-Pedrajo, N. Kami-ike, and K. Namba. 2009. Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus. Mol. Microbiol. 74:1471-1483.
    • (2009) Mol. Microbiol , vol.74 , pp. 1471-1483
    • Minamino, T.1    Yoshimura, S.D.J.2    Morimoto, Y.V.3    González-Pedrajo, B.4    Kami-ike, N.5    Namba, K.6
  • 25
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium
    • Ohnishi, K., Y. Ohto, S.-I. Aizawa, R. M. Macnab, and T. Iino. 1994. FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J. Bacteriol. 176:2272-2281.
    • (1994) J. Bacteriol , vol.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohto, Y.2    Aizawa, S.-I.3    Macnab, R.M.4    Iino, T.5
  • 26
    • 0030983817 scopus 로고    scopus 로고
    • Ohnishi, K., F. Fan, G. J. Schoenhals, M. Kihara, and R. M. Macnab. 1997. The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: putative components for flagellar assembly. J. Bacteriol. 179:6092-6099.
    • Ohnishi, K., F. Fan, G. J. Schoenhals, M. Kihara, and R. M. Macnab. 1997. The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: putative components for flagellar assembly. J. Bacteriol. 179:6092-6099.
  • 27
  • 28
    • 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., T. Minamino, R. M. Macnab, and K. Namba. 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
  • 30
    • 1842454268 scopus 로고    scopus 로고
    • Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB
    • Van Arnam, J. S., J. L. McMurry, M. Kihara, and R. M. Macnab. 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
  • 31
    • 0022899744 scopus 로고
    • Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium
    • Yamaguchi, S., S.-I. Aizawa, M. Kihara, M. Isomura, C. J. Jones, and R. M. Macnab. 1986. Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium. J. Bacteriol. 168:1172-1179.
    • (1986) J. Bacteriol , vol.168 , pp. 1172-1179
    • Yamaguchi, S.1    Aizawa, S.-I.2    Kihara, M.3    Isomura, M.4    Jones, C.J.5    Macnab, R.M.6
  • 32
    • 0021347115 scopus 로고
    • Genetic analysis of H2, the structural gene for phase-2 flagellin in Salmonella
    • Yamaguchi, S., H. Fujita, K. Sugata, T. Taira, and T. Iino. 1984. Genetic analysis of H2, the structural gene for phase-2 flagellin in Salmonella. J. Gen. Microbiol. 130:255-265.
    • (1984) J. Gen. Microbiol , vol.130 , pp. 255-265
    • Yamaguchi, S.1    Fujita, H.2    Sugata, K.3    Taira, T.4    Iino, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.