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Volumn 28, Issue 4, 2009, Pages 315-325

Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion

Author keywords

AAA+ protein; Chaperone; Protein secretion

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CHAPERONE; PROTEIN AAA; PROTEIN C1PV; PROTEIN HCP; PROTEIN VGRG; PROTEIN VIPA; PROTEIN VIPB; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

EID: 60549104572     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2008.269     Document Type: Article
Times cited : (263)

References (47)
  • 1
    • 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
  • 2
    • 0037214659 scopus 로고    scopus 로고
    • Infection-blocking genes of a symbiotic Rhizobium leguminosarum strain that are involved in temperature-dependent protein secretion
    • Bladergroen MR, Badelt K, Spaink HP (2003) Infection-blocking genes of a symbiotic Rhizobium leguminosarum strain that are involved in temperature-dependent protein secretion. Mol Plant Microbe Interact 16: 53-64
    • (2003) Mol Plant Microbe Interact , vol.16 , pp. 53-64
    • Bladergroen, M.R.1    Badelt, K.2    Spaink, H.P.3
  • 3
    • 48649107476 scopus 로고    scopus 로고
    • The type VI secretion toolkit
    • Cascales E (2008) The type VI secretion toolkit. EMBO Rep 9: 735-741
    • (2008) EMBO Rep , vol.9 , pp. 735-741
    • Cascales, E.1
  • 4
    • 0345602998 scopus 로고    scopus 로고
    • Identification of a unique IAHP (IcmF associated homologous proteins) cluster in Vibrio cholerae and other proteobacteria through in silico analysis
    • Das S, Chaudhuri K (2003) Identification of a unique IAHP (IcmF associated homologous proteins) cluster in Vibrio cholerae and other proteobacteria through in silico analysis. In Silico Biol 3: 287-300
    • (2003) In Silico Biol , vol.3 , pp. 287-300
    • Das, S.1    Chaudhuri, K.2
  • 5
    • 33846845100 scopus 로고    scopus 로고
    • The Francisella pathogenicity island protein IglA localizes to the bacterial cytoplasm and is needed for intracellular growth
    • de Bruin OM, Ludu JS, Nano FE (2007) The Francisella pathogenicity island protein IglA localizes to the bacterial cytoplasm and is needed for intracellular growth. BMC Microbiol 7: 1
    • (2007) BMC Microbiol , vol.7 , pp. 1
    • de Bruin, O.M.1    Ludu, J.S.2    Nano, F.E.3
  • 6
    • 33749234149 scopus 로고    scopus 로고
    • Modeling AAA+ ring complexes from monomeric structures
    • Diemand AV, Lupas AN (2006) Modeling AAA+ ring complexes from monomeric structures. J Struct Biol 156: 230-243
    • (2006) J Struct Biol , vol.156 , pp. 230-243
    • Diemand, A.V.1    Lupas, A.N.2
  • 7
    • 3242879177 scopus 로고    scopus 로고
    • iMolTalk: An interactive, internet-based protein structure analysis server
    • Diemand AV, Scheib H (2004) iMolTalk: an interactive, internet-based protein structure analysis server. Nucleic Acids Res 32: W512-W516
    • (2004) Nucleic Acids Res , vol.32
    • Diemand, A.V.1    Scheib, H.2
  • 8
    • 33747080208 scopus 로고    scopus 로고
    • Proteomic and microarray characterization of the AggR regulon identifies a pheU pathogenicity island in enteroaggregative Escherichia coli
    • Dudley EG, Thomson NR, Parkhill J, Morin NP, Nataro JP (2006) Proteomic and microarray characterization of the AggR regulon identifies a pheU pathogenicity island in enteroaggregative Escherichia coli. Mol Microbiol 61: 1267-1282
    • (2006) Mol Microbiol , vol.61 , pp. 1267-1282
    • Dudley, E.G.1    Thomson, N.R.2    Parkhill, J.3    Morin, N.P.4    Nataro, J.P.5
  • 9
    • 14544306021 scopus 로고    scopus 로고
    • Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolyticus
    • Enos-Berlage JL, Guvener ZT, Keenan CE, McCarter LL (2005) Genetic determinants of biofilm development of opaque and translucent Vibrio parahaemolyticus. Mol Microbiol 55: 1160-1182
    • (2005) Mol Microbiol , vol.55 , pp. 1160-1182
    • Enos-Berlage, J.L.1    Guvener, Z.T.2    Keenan, C.E.3    McCarter, L.L.4
  • 11
    • 48449086943 scopus 로고    scopus 로고
    • The bacterial type VI secretion machine: Yet another player for protein transport across membranes
    • Filloux A, Hachani A, Bleves S (2008) The bacterial type VI secretion machine: yet another player for protein transport across membranes. Microbiology 154: 1570-1583
    • (2008) Microbiology , vol.154 , pp. 1570-1583
    • Filloux, A.1    Hachani, A.2    Bleves, S.3
  • 12
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan JE, Wolf-Watz H (2006) Protein delivery into eukaryotic cells by type III secretion machines. Nature 444: 567-573
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 14
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 15
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • Guo F, Maurizi MR, Esser L, Xia D (2002) Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J Biol Chem 277: 46743-46752
    • (2002) J Biol Chem , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 16
    • 0029198455 scopus 로고
    • A simple and rapid method for transformation of Vibrio species by electroporation
    • Hamashima H, Iwasaki M, Arai T (1995) A simple and rapid method for transformation of Vibrio species by electroporation. Methods Mol Biol 47: 155-160
    • (1995) Methods Mol Biol , vol.47 , pp. 155-160
    • Hamashima, H.1    Iwasaki, M.2    Arai, T.3
  • 19
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch J, Fenton WA, Furtak KJ, Farr GW, Horwich AL (2005) Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121: 1029-1041
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 20
    • 0344629876 scopus 로고    scopus 로고
    • Structure and function of the middle domain of ClpB from Escherichia coli
    • Kedzierska S, Akoev V, Barnett ME, Zolkiewski M (2003) Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry 42: 14242-14248
    • (2003) Biochemistry , vol.42 , pp. 14242-14248
    • Kedzierska, S.1    Akoev, V.2    Barnett, M.E.3    Zolkiewski, M.4
  • 22
    • 34347389638 scopus 로고    scopus 로고
    • Threonine phosphorylation times bacterial secretion
    • Kulasekara HD, Miller SI (2007) Threonine phosphorylation times bacterial secretion. Nat Cell Biol 9: 734-736
    • (2007) Nat Cell Biol , vol.9 , pp. 734-736
    • Kulasekara, H.D.1    Miller, S.I.2
  • 24
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state
    • Lee S, Sowa ME, Watanabe Y, Sigler PB, Chiu W, Yoshida M, Tsai FT (2003) The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state. Cell 115: 229-240
    • (2003) Cell , vol.115 , pp. 229-240
    • Lee, S.1    Sowa, M.E.2    Watanabe, Y.3    Sigler, P.B.4    Chiu, W.5    Yoshida, M.6    Tsai, F.T.7
  • 25
    • 0037705402 scopus 로고    scopus 로고
    • Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP-hydrolysis and chaperone activity
    • Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B (2003) Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP-hydrolysis and chaperone activity. J Biol Chem 278: 15-24
    • (2003) J Biol Chem , vol.278 , pp. 15-24
    • Mogk, A.1    Schlieker, C.2    Strub, C.3    Rist, W.4    Weibezahn, J.5    Bukau, B.6
  • 28
    • 21544479117 scopus 로고    scopus 로고
    • sciS, an icmF homolog in Salmonella enterica serovar typhimurium, limits intracellular replication and decreases virulence
    • Parsons DA, Heffron F (2005) sciS, an icmF homolog in Salmonella enterica serovar typhimurium, limits intracellular replication and decreases virulence. Infect Immun 73: 4338-4345
    • (2005) Infect Immun , vol.73 , pp. 4338-4345
    • Parsons, D.A.1    Heffron, F.2
  • 29
    • 1942487190 scopus 로고    scopus 로고
    • Improvement of pCVD442, a suicide plasmid for gene allele exchange in bacteria
    • Philippe N, Alcaraz JP, Coursange E, Geiselmann J, Schneider D (2004) Improvement of pCVD442, a suicide plasmid for gene allele exchange in bacteria. Plasmid 51: 246-255
    • (2004) Plasmid , vol.51 , pp. 246-255
    • Philippe, N.1    Alcaraz, J.P.2    Coursange, E.3    Geiselmann, J.4    Schneider, D.5
  • 30
    • 34848882221 scopus 로고    scopus 로고
    • Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin
    • Pukatzki S, Ma AT, Revel AT, Sturtevant D, Mekalanos JJ (2007) Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin. Proc Natl Acad Sci USA 104: 15508-15513
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15508-15513
    • Pukatzki, S.1    Ma, A.T.2    Revel, A.T.3    Sturtevant, D.4    Mekalanos, J.J.5
  • 32
    • 3242890783 scopus 로고    scopus 로고
    • Use of proteomics to identify novel virulence determinants that are required for Edwardsiella tarda pathogenesis
    • Rao PS, Yamada Y, Tan YP, Leung KY (2004) Use of proteomics to identify novel virulence determinants that are required for Edwardsiella tarda pathogenesis. Mol Microbiol 53: 573-586
    • (2004) Mol Microbiol , vol.53 , pp. 573-586
    • Rao, P.S.1    Yamada, Y.2    Tan, Y.P.3    Leung, K.Y.4
  • 33
    • 1842861589 scopus 로고    scopus 로고
    • Structural biology of bacterial pathogenesis
    • Remaut H, Waksman G (2004) Structural biology of bacterial pathogenesis. Curr Opin Struct Biol 14: 161-170
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 161-170
    • Remaut, H.1    Waksman, G.2
  • 34
    • 38349097870 scopus 로고    scopus 로고
    • Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
    • Roll-Mecak A, Vale RD (2008) Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature 451: 363-367
    • (2008) Nature , vol.451 , pp. 363-367
    • Roll-Mecak, A.1    Vale, R.D.2
  • 35
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 38
    • 28244467883 scopus 로고    scopus 로고
    • ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria
    • Schlieker C, Zentgraf H, Dersch P, Mogk A (2005) ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria. Biol Chem 386: 1115-1127
    • (2005) Biol Chem , vol.386 , pp. 1115-1127
    • Schlieker, C.1    Zentgraf, H.2    Dersch, P.3    Mogk, A.4
  • 39
    • 1542283751 scopus 로고    scopus 로고
    • Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates
    • Siddiqui SM, Sauer RT, Baker TA (2004) Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. Genes Dev 18: 369-374
    • (2004) Genes Dev , vol.18 , pp. 369-374
    • Siddiqui, S.M.1    Sauer, R.T.2    Baker, T.A.3
  • 40
    • 40649098449 scopus 로고    scopus 로고
    • Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
    • Tessarz P, Mogk A, Bukau B (2008) Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol Microbiol 68: 87-97
    • (2008) Mol Microbiol , vol.68 , pp. 87-97
    • Tessarz, P.1    Mogk, A.2    Bukau, B.3
  • 43
    • 41949130225 scopus 로고    scopus 로고
    • Secretome analysis uncovers an Hcp-family protein secreted via a type VI secretion system in Agrobacterium tumefaciens
    • Wu HY, Chung PC, Shih HW, Wen SR, Lai EM (2008) Secretome analysis uncovers an Hcp-family protein secreted via a type VI secretion system in Agrobacterium tumefaciens. J Bacteriol 190: 2841-2850
    • (2008) J Bacteriol , vol.190 , pp. 2841-2850
    • Wu, H.Y.1    Chung, P.C.2    Shih, H.W.3    Wen, S.R.4    Lai, E.M.5
  • 44
    • 1242278245 scopus 로고    scopus 로고
    • Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone
    • Xia D, Esser L, Singh SK, Guo F, Maurizi MR (2004) Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone. J Struct Biol 146: 166-179
    • (2004) J Struct Biol , vol.146 , pp. 166-179
    • Xia, D.1    Esser, L.2    Singh, S.K.3    Guo, F.4    Maurizi, M.R.5
  • 45
    • 0348010363 scopus 로고    scopus 로고
    • Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis
    • Yamada-Inagawa T, Okuno T, Karata K, Yamanaka K, Ogura T (2003) Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis. J Biol Chem 278: 50182-50187
    • (2003) J Biol Chem , vol.278 , pp. 50182-50187
    • Yamada-Inagawa, T.1    Okuno, T.2    Karata, K.3    Yamanaka, K.4    Ogura, T.5
  • 46
    • 1642415666 scopus 로고    scopus 로고
    • Unveiling molecular scaffolds of the type IV secretion system
    • Yeo HJ, Waksman G (2004) Unveiling molecular scaffolds of the type IV secretion system. J Bacteriol 186: 1919-1926
    • (2004) J Bacteriol , vol.186 , pp. 1919-1926
    • Yeo, H.J.1    Waksman, G.2
  • 47
    • 36148956564 scopus 로고    scopus 로고
    • Dissection of a type VI secretion system in Edwardsiella tarda
    • Zheng J, Leung KY (2007) Dissection of a type VI secretion system in Edwardsiella tarda. Mol Microbiol 66: 1192-1206
    • (2007) Mol Microbiol , vol.66 , pp. 1192-1206
    • Zheng, J.1    Leung, K.Y.2


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