메뉴 건너뛰기




Volumn 113, Issue 13, 2016, Pages 3633-3638

Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator

Author keywords

Bacterial flagellum; Crystal structure; F A V type ATPase; Type III protein export

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HOMODIMER; BACTERIAL PROTEIN; FLIH PROTEIN, BACTERIA; FLII PROTEIN, BACTERIA; FLIJ PROTEIN, BACTERIA; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; TYPE III SECRETION SYSTEM;

EID: 84962106823     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1524025113     Document Type: Article
Times cited : (51)

References (50)
  • 1
    • 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(1-3):207-217.
    • (2004) Biochim Biophys Acta , vol.1694 , Issue.1-3 , pp. 207-217
    • Macnab, R.M.1
  • 2
    • 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 Microbiol Biotechnol 7(1-2):5-17.
    • (2004) J Mol Microbiol Biotechnol , vol.7 , Issue.1-2 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 3
    • 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(4):1105-1115.
    • (2008) Mol Biosyst , vol.4 , Issue.4 , pp. 1105-1115
    • Minamino, T.1    Imada, K.2    Namba, K.3
  • 4
    • 84902327129 scopus 로고    scopus 로고
    • Protein export through the bacterial flagellar type III export pathway
    • Minamino T (2014) Protein export through the bacterial flagellar type III export pathway. Biochim Biophys Acta 1843(1843):1642-1648.
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.1843 , pp. 1642-1648
    • Minamino, T.1
  • 5
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis GR (2006) The type III secretion injectisome. Nat Rev Microbiol 4(4):811-825.
    • (2006) Nat Rev Microbiol , vol.4 , Issue.4 , pp. 811-825
    • Cornelis, G.R.1
  • 6
    • 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(271):31981-31988.
    • (1996) J Biol Chem , vol.271 , Issue.271 , pp. 31981-31988
    • Fan, F.1    Macnab, R.M.2
  • 7
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret L, Calder SR, Higgins M, Hughes C (2003) Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol Microbiol 48(48):1349-1355.
    • (2003) Mol Microbiol , vol.48 , Issue.48 , pp. 1349-1355
    • Claret, L.1    Calder, S.R.2    Higgins, M.3    Hughes, C.4
  • 8
    • 33745276514 scopus 로고    scopus 로고
    • Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region
    • Minamino T, et al. (2006) Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region. J Mol Biol 360(360):510-519.
    • (2006) J Mol Biol , vol.360 , Issue.360 , pp. 510-519
    • Minamino, T.1
  • 9
    • 79960620016 scopus 로고    scopus 로고
    • Structural diversity of bacterial flagellar motors
    • Chen S, et al. (2011) Structural diversity of bacterial flagellar motors. EMBO J 30(30): 2972-2981.
    • (2011) EMBO J , vol.30 , Issue.30 , pp. 2972-2981
    • Chen, S.1
  • 10
    • 33646435299 scopus 로고    scopus 로고
    • Interactions between C ring proteins and export apparatus components: A possible mechanism for facilitating type III protein export
    • González-Pedrajo B, Minamino T, Kihara M, Namba K (2006) Interactions between C ring proteins and export apparatus components: A possible mechanism for facilitating type III protein export. Mol Microbiol 60(60):984-998.
    • (2006) Mol Microbiol , vol.60 , Issue.60 , pp. 984-998
    • González-Pedrajo, B.1    Minamino, T.2    Kihara, M.3    Namba, K.4
  • 11
    • 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, et al. (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(74):1471-1483.
    • (2009) Mol Microbiol , vol.74 , Issue.74 , pp. 1471-1483
    • Minamino, T.1
  • 12
    • 84923284551 scopus 로고    scopus 로고
    • Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus
    • Bai F, et al. (2014) Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus. Sci Rep 4:6528.
    • (2014) Sci Rep , vol.4 , pp. 6528
    • Bai, F.1
  • 14
    • 79952359941 scopus 로고    scopus 로고
    • Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases
    • Ibuki T, et al. (2011) Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases. Nat Struct Mol Biol 18(18):277-282.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.18 , pp. 277-282
    • Ibuki, T.1
  • 15
    • 84878377906 scopus 로고    scopus 로고
    • Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus
    • Kishikawa J, et al. (2013) Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus. PLoS One 8(8):e64695.
    • (2013) PLoS One , vol.8 , Issue.8
    • Kishikawa, J.1
  • 16
    • 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(451):485-488.
    • (2008) Nature , vol.451 , Issue.451 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 17
    • 38549088345 scopus 로고    scopus 로고
    • Energy source of flagellar type III secretion
    • Paul K, Erhardt M, Hirano T, Blair DF, Hughes KT (2008) Energy source of flagellar type III secretion. Nature 451(451):489-492.
    • (2008) Nature , vol.451 , Issue.451 , pp. 489-492
    • Paul, K.1    Erhardt, M.2    Hirano, T.3    Blair, D.F.4    Hughes, K.T.5
  • 18
    • 80053415915 scopus 로고    scopus 로고
    • An energy transduction mechanism used in bacterial flagellar type III protein export
    • Minamino T, Morimoto YV, Hara N, Namba K (2011) An energy transduction mechanism used in bacterial flagellar type III protein export. Nat Commun 2:475.
    • (2011) Nat Commun , vol.2 , pp. 475
    • Minamino, T.1    Morimoto, Y.V.2    Hara, N.3    Namba, K.4
  • 19
    • 84923371148 scopus 로고    scopus 로고
    • The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis
    • Minamino T, Morimoto YV, Kinoshita M, Aldridge PD, Namba K (2014) The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis. Sci Rep 4:7579.
    • (2014) Sci Rep , vol.4 , pp. 7579
    • Minamino, T.1    Morimoto, Y.V.2    Kinoshita, M.3    Aldridge, P.D.4    Namba, K.5
  • 20
    • 0033779545 scopus 로고    scopus 로고
    • Fli H, 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) Fli H, 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(37):1494-1503.
    • (2000) Mol Microbiol , vol.37 , Issue.37 , pp. 1494-1503
    • Minamino, T.1    Macnab, R.M.2
  • 21
    • 0036041918 scopus 로고    scopus 로고
    • Molecular dissection of salmonella fli H, a regulator of the ATPase FliI and the type III flagellar protein export pathway
    • González-Pedrajo B, Fraser GM, Minamino T, Macnab RM (2002) Molecular dissection of Salmonella Fli H, a regulator of the ATPase FliI and the type III flagellar protein export pathway. Mol Microbiol 45(45):967-982.
    • (2002) Mol Microbiol , vol.45 , Issue.45 , pp. 967-982
    • González-Pedrajo, B.1    Fraser, G.M.2    Minamino, T.3    Macnab, R.M.4
  • 22
    • 59849126764 scopus 로고    scopus 로고
    • Role of the N-terminal domain of FliI ATPase in bacterial flagellar protein export
    • Okabe M, Minamino T, Imada K, Namba K, Kihara M (2009) Role of the N-terminal domain of FliI ATPase in bacterial flagellar protein export. FEBS Lett 583(583):743-748.
    • (2009) FEBS Lett , vol.583 , Issue.583 , pp. 743-748
    • Okabe, M.1    Minamino, T.2    Imada, K.3    Namba, K.4    Kihara, M.5
  • 23
    • 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(101):3945-3950.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 24
    • 77952710839 scopus 로고    scopus 로고
    • Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners
    • Imada K, Minamino T, Kinoshita M, Furukawa Y, Namba K (2010) Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proc Natl Acad Sci USA 107(107):8812-8817.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.107 , pp. 8812-8817
    • Imada, K.1    Minamino, T.2    Kinoshita, M.3    Furukawa, Y.4    Namba, K.5
  • 25
    • 84155162801 scopus 로고    scopus 로고
    • Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export
    • Minamino T, Kinoshita M, Imada K, Namba K (2012) Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export. Mol Microbiol 83(83):168-178.
    • (2012) Mol Microbiol , vol.83 , Issue.83 , pp. 168-178
    • Minamino, T.1    Kinoshita, M.2    Imada, K.3    Namba, K.4
  • 26
    • 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(35):1052-1064.
    • (2000) Mol Microbiol , vol.35 , Issue.35 , pp. 1052-1064
    • Minamino, T.1    Macnab, R.M.2
  • 27
    • 84868305790 scopus 로고    scopus 로고
    • Interaction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein export
    • Hara N, Morimoto YV, Kawamoto A, Namba K, Minamino T (2012) Interaction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein export. J Bacteriol 194(194):5353-5360.
    • (2012) J Bacteriol , vol.194 , Issue.194 , pp. 5353-5360
    • Hara, N.1    Morimoto, Y.V.2    Kawamoto, A.3    Namba, K.4    Minamino, T.5
  • 28
    • 0036384413 scopus 로고    scopus 로고
    • Structural properties of fli H, an ATPase regulatory component of the salmonella type III flagellar export apparatus
    • Minamino T, González-Pedrajo B, Oosawa K, Namba K, Macnab RM (2002) Structural properties of Fli H, an ATPase regulatory component of the Salmonella type III flagellar export apparatus. J Mol Biol 322(322):281-290.
    • (2002) J Mol Biol , vol.322 , Issue.322 , pp. 281-290
    • Minamino, T.1    González-Pedrajo, B.2    Oosawa, K.3    Namba, K.4    Macnab, R.M.5
  • 29
    • 33645519210 scopus 로고    scopus 로고
    • Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoF1 and vacuolar ATPases
    • Pallen MJ, Bailey CM, Beatson SA (2006) Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoF1 and vacuolar ATPases. Protein Sci 15(15):935-941.
    • (2006) Protein Sci , vol.15 , Issue.15 , pp. 935-941
    • Pallen, M.J.1    Bailey, C.M.2    Beatson, S.A.3
  • 30
    • 84869004614 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the FliH-flii complex responsible for bacterial flagellar type III protein export
    • Uchida Y, Minamino T, Namba K, Imada K (2012) Crystallization and preliminary X-ray analysis of the FliH-FliI complex responsible for bacterial flagellar type III protein export. Acta Crystallogr Sect F Struct Biol Cryst Commun 68(Pt 11):1311-1314.
    • (2012) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.68 , pp. 1311-1314
    • Uchida, Y.1    Minamino, T.2    Namba, K.3    Imada, K.4
  • 33
    • 0035812653 scopus 로고    scopus 로고
    • Proteolytic analysis of the FliH/FliI complex, the ATPase component of the type III flagellar export apparatus of salmonella
    • Minamino T, Tame JR, Namba K, Macnab RM (2001) Proteolytic analysis of the FliH/FliI complex, the ATPase component of the type III flagellar export apparatus of Salmonella. J Mol Biol 312(312):1027-1036.
    • (2001) J Mol Biol , vol.312 , Issue.312 , pp. 1027-1036
    • Minamino, T.1    Tame, J.R.2    Namba, K.3    Macnab, R.M.4
  • 34
    • 84922223631 scopus 로고    scopus 로고
    • Visualization of the type III secretion sorting platform of shigella flexneri
    • Hu B, et al. (2015) Visualization of the type III secretion sorting platform of Shigella flexneri. Proc Natl Acad Sci USA 112(112):1047-1052.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.112 , pp. 1047-1052
    • Hu, B.1
  • 35
    • 84889777894 scopus 로고    scopus 로고
    • Common and distinct structural features of salmonella injectisome and flagellar basal body
    • Kawamoto A, et al. (2013) Common and distinct structural features of Salmonella injectisome and flagellar basal body. Sci Rep 3:3369.
    • (2013) Sci Rep , vol.3 , pp. 3369
    • Kawamoto, A.1
  • 36
    • 84936935603 scopus 로고    scopus 로고
    • Mutations in the borrelia burgdorferi flagellar type III secretion system genes fliH and fliI profoundly affect spirochete flagellar assembly, morphology, motility, structure, and cell division
    • Lin T, Gao L, Zhao X, Liu J, Norris SJ (2015) Mutations in the Borrelia burgdorferi flagellar type III secretion system genes fliH and fliI profoundly affect spirochete flagellar assembly, morphology, motility, structure, and cell division. MBio 6(6):e00579-15.
    • (2015) MBio , vol.6 , Issue.6
    • Lin, T.1    Gao, L.2    Zhao, X.3    Liu, J.4    Norris, S.J.5
  • 37
    • 84930224980 scopus 로고    scopus 로고
    • A common assembly module in injectisome and flagellar type III secretion sorting platforms
    • Notti RQ, Bhattacharya S, Lilic M, Stebbins CE (2015) A common assembly module in injectisome and flagellar type III secretion sorting platforms. Nat Commun 6:7125.
    • (2015) Nat Commun , vol.6 , pp. 7125
    • Notti, R.Q.1    Bhattacharya, S.2    Lilic, M.3    Stebbins, C.E.4
  • 38
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams JP, Leslie AGW, Lutter R, Walker JE (1994) Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370(370):621-628.
    • (1994) Nature , vol.370 , Issue.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 39
    • 84873657291 scopus 로고    scopus 로고
    • Rotation mechanism of enterococcus hirae V1-ATPase based on asymmetric crystal structures
    • Arai S, et al. (2013) Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures. Nature 493(493):703-707.
    • (2013) Nature , vol.493 , Issue.493 , pp. 703-707
    • Arai, S.1
  • 40
    • 4644290116 scopus 로고    scopus 로고
    • +-ATPase/synthase by electron microscopy
    • +-ATPase/synthase by electron microscopy. Structure 12(12):1789-1798.
    • (2004) Structure , vol.12 , Issue.12 , pp. 1789-1798
    • Bernal, R.A.1    Stock, D.2
  • 41
    • 0037059613 scopus 로고    scopus 로고
    • Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer
    • Deo RC, Groft CM, Rajashankar KR, Burley SK (2002) Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer. Cell 108(108):71-81.
    • (2002) Cell , vol.108 , Issue.108 , pp. 71-81
    • Deo, R.C.1    Groft, C.M.2    Rajashankar, K.R.3    Burley, S.K.4
  • 42
    • 84861324339 scopus 로고    scopus 로고
    • Extent of structural asymmetry in homodimeric proteins: Prevalence and relevance
    • Swapna LS, Srikeerthana K, Srinivasan N (2012) Extent of structural asymmetry in homodimeric proteins: Prevalence and relevance. PLoS One 7(7):e36688.
    • (2012) PLoS One , vol.7 , Issue.7
    • Swapna, L.S.1    Srikeerthana, K.2    Srinivasan, N.3
  • 43
    • 84868582759 scopus 로고    scopus 로고
    • Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex
    • Oot RA, Huang LS, Berry EA, Wilkens S (2012) Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex. Structure 20(20):1881-1892.
    • (2012) Structure , vol.20 , Issue.20 , pp. 1881-1892
    • Oot, R.A.1    Huang, L.S.2    Berry, E.A.3    Wilkens, S.4
  • 44
    • 76049093135 scopus 로고    scopus 로고
    • The structure of the membrane extrinsic region of bovine ATP synthase
    • Rees DM, Leslie AGW, Walker JE (2009) The structure of the membrane extrinsic region of bovine ATP synthase. Proc Natl Acad Sci USA 106(106):21597-21601.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.106 , pp. 21597-21601
    • Rees, D.M.1    Leslie, A.G.2    Walker, J.E.3
  • 45
    • 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(181):1388-1394.
    • (1999) J Bacteriol , vol.181 , Issue.181 , pp. 1388-1394
    • Minamino, T.1    Macnab, R.M.2
  • 46
    • 71649092785 scopus 로고    scopus 로고
    • Processing diffraction data with mosflm
    • NATO Science Series, eds Read RJ, Sussman JL (Springer, Dordrecht, The Netherlands)
    • Leslie AGW, Powell HR (2007) Processing diffraction data with Mosflm. Evolving Methods for Macromolecular Crystallography, NATO Science Series, eds Read RJ, Sussman JL (Springer, Dordrecht, The Netherlands), Vol 245, pp 41-51.
    • (2007) Evolving Methods for Macromolecular Crystallography , vol.245 , pp. 41-51
    • Leslie, A.G.1    Powell, H.R.2
  • 47
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67(Pt 4):235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 48
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58(Pt 11):1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 49
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 50
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in salmonella typhimurium
    • Ohnishi K, Ohto Y, Aizawa S, Macnab RM, Iino T (1994) FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J Bacteriol 176(176):2272-2281.
    • (1994) J Bacteriol , vol.176 , Issue.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohto, Y.2    Aizawa, S.3    Macnab, R.M.4    Iino, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.