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Volumn 190, Issue 20, 2008, Pages 6580-6588

Characterization of the putative type III secretion ATPase CdsN (Cpn0707) of Chlamydophila pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; CDSD ADENOSINE TRIPHOSPHATASE; CDSN ADENOSINE TRIPHOSPHATASE; CDSQ ADENOSINE TRIPHOSPHATASE; CHAPERONE; COPN ADENOSINE TRIPHOSPHATASE; GLUTATHIONE TRANSFERASE; OLIGOMER; UNCLASSIFIED DRUG;

EID: 53849145648     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00761-08     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda, Y., and J. Galan. 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.2
  • 2
    • 1842506700 scopus 로고    scopus 로고
    • Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains
    • Akeda, Y., and J. Galan. 2004. Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains. J. Bacteriol. 186:2402-2412.
    • (2004) J. Bacteriol , vol.186 , pp. 2402-2412
    • Akeda, Y.1    Galan, J.2
  • 4
    • 39749143271 scopus 로고    scopus 로고
    • Bioinformatic and biochemical evidence for the identification of the type III secretion system Needle protein of Chlamydia trachomatis
    • Betts, H., L. Twiggs, M. Sal, P. Wyrick, and K. Fields. 2008. Bioinformatic and biochemical evidence for the identification of the type III secretion system Needle protein of Chlamydia trachomatis. J. Bacteriol. 190:1680-1690.
    • (2008) J. Bacteriol , vol.190 , pp. 1680-1690
    • Betts, H.1    Twiggs, L.2    Sal, M.3    Wyrick, P.4    Fields, K.5
  • 5
    • 33646543996 scopus 로고    scopus 로고
    • Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL
    • Blaylock, B., K. Riordan, D. Missiakas, and O. Schneewind. 2006. Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL. J. Bacteriol. 188:3525-3534.
    • (2006) J. Bacteriol , vol.188 , pp. 3525-3534
    • Blaylock, B.1    Riordan, K.2    Missiakas, D.3    Schneewind, O.4
  • 6
    • 2942667797 scopus 로고    scopus 로고
    • Requirement for the Rac GTPase in Chlamydia trachomatis invasion of non-phagocytic cells
    • Carabeo, R., S. Grieshaber, A. Hasenkrug, C. Dooley, and T. Hackstadt. 2004. Requirement for the Rac GTPase in Chlamydia trachomatis invasion of non-phagocytic cells. Traffic 5:418-425.
    • (2004) Traffic , vol.5 , pp. 418-425
    • Carabeo, R.1    Grieshaber, S.2    Hasenkrug, A.3    Dooley, C.4    Hackstadt, T.5
  • 7
    • 3042707297 scopus 로고    scopus 로고
    • A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin
    • Clifton, D., K. Fields, S. Grieshaber, C. Dooley, E. Fischer, D. Mead, R. Carabeo, and T. Hackstadt. 2004. A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin. Proc. Natl. Acad. Sci. USA 101:10166-10171.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10166-10171
    • Clifton, D.1    Fields, K.2    Grieshaber, S.3    Dooley, C.4    Fischer, E.5    Mead, D.6    Carabeo, R.7    Hackstadt, T.8
  • 8
    • 0036326980 scopus 로고    scopus 로고
    • Identification of MEK- and phosphoinositide-3-kinase-dependant signaling as essential events during Chlamydia pneumoniae invasion of HEp2 cells
    • Coombes, B., and J. Mahony. 2002. Identification of MEK- and phosphoinositide-3-kinase-dependant signaling as essential events during Chlamydia pneumoniae invasion of HEp2 cells. Cell. Microbiol. 4:447-460.
    • (2002) Cell. Microbiol , vol.4 , pp. 447-460
    • Coombes, B.1    Mahony, J.2
  • 9
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis, G. 2006. The type III secretion injectisome. Nat. Rev. Microbiol. 4:811-825.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 811-825
    • Cornelis, G.1
  • 10
    • 0034533953 scopus 로고    scopus 로고
    • Evidence for the secretion of Chlamydia trachomatis CopN by a type III secretion mechanism
    • Fields, K., and T. Hackstadt. 2000. Evidence for the secretion of Chlamydia trachomatis CopN by a type III secretion mechanism. Mol. Microbiol. 38:1048-1060.
    • (2000) Mol. Microbiol , vol.38 , pp. 1048-1060
    • Fields, K.1    Hackstadt, T.2
  • 11
    • 0038011417 scopus 로고    scopus 로고
    • Chlamydia trachomatis type III secretion: Evidence for a functional apparatus during earlycycle development
    • Fields, K., D. Mead, C. Dooley, and T. Hackstadt. 2003. Chlamydia trachomatis type III secretion: evidence for a functional apparatus during earlycycle development. Mol. Microbiol. 48:671-683.
    • (2003) Mol. Microbiol , vol.48 , pp. 671-683
    • Fields, K.1    Mead, D.2    Dooley, C.3    Hackstadt, T.4
  • 12
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • Galan, J., and A. Collmer. 1999. Type III secretion machines: bacterial devices for protein delivery into host cells. Science 284:1322-1328.
    • (1999) Science , vol.284 , pp. 1322-1328
    • Galan, J.1    Collmer, A.2
  • 13
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan, J., and H. Wolf-Watz. 2006. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444:567-573.
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.1    Wolf-Watz, H.2
  • 14
    • 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., and B. Finlay. 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.2
  • 15
    • 10344249890 scopus 로고    scopus 로고
    • Process of protein transport by the type III secretion system
    • Ghosh, P. 2004. Process of protein transport by the type III secretion system. Microbiol. Mol. Biol. Rev. 68:771-795.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 771-795
    • Ghosh, P.1
  • 16
    • 33845919357 scopus 로고    scopus 로고
    • Chlamydial type III secretion system is encoded on ten operons preceded by sigma 70-like promoter elements
    • Hefty, P., and R. Stephens. 2007. Chlamydial type III secretion system is encoded on ten operons preceded by sigma 70-like promoter elements. J. Bacteriol. 189:198-206.
    • (2007) J. Bacteriol , vol.189 , pp. 198-206
    • Hefty, P.1    Stephens, R.2
  • 17
    • 33745999156 scopus 로고    scopus 로고
    • Identification and characterization of secreted effector proteins of Chlamydophila pneumoniae TW183
    • Herrmann, M., A. Schuhmacher, I. Muhldorfer, K. Melchers, C. Prothmann, and S. Dammeier. 2006. Identification and characterization of secreted effector proteins of Chlamydophila pneumoniae TW183. Res. Microbiol. 157:513-524.
    • (2006) Res. Microbiol , vol.157 , pp. 513-524
    • Herrmann, M.1    Schuhmacher, A.2    Muhldorfer, I.3    Melchers, K.4    Prothmann, C.5    Dammeier, S.6
  • 18
    • 40149087043 scopus 로고    scopus 로고
    • Spatial constraints within the chlamydial host cell inclusion predict interrupted development and persistence
    • Hoare, A., P. Timms, P. Bavoil, and D. Wilson. 2008. Spatial constraints within the chlamydial host cell inclusion predict interrupted development and persistence. BMC Microbiol. 8:5.
    • (2008) BMC Microbiol , vol.8 , pp. 5
    • Hoare, A.1    Timms, P.2    Bavoil, P.3    Wilson, D.4
  • 19
    • 0030877189 scopus 로고    scopus 로고
    • Type III secretion genes identify a putative virulence locus of Chlamydia
    • Hsia, R., Y. Pannekoek, E. Ingerowski, and P. Bavoil. 1997. Type III secretion genes identify a putative virulence locus of Chlamydia. Mol. Microbiol. 23:351-359.
    • (1997) Mol. Microbiol , vol.23 , pp. 351-359
    • Hsia, R.1    Pannekoek, Y.2    Ingerowski, E.3    Bavoil, P.4
  • 20
    • 0031864184 scopus 로고    scopus 로고
    • Type III secretion systems in bacterial pathogens of animals and plants
    • Hueck, C. 1998. Type III 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.1
  • 21
    • 34547397847 scopus 로고    scopus 로고
    • Mechanisms of host cell exit by the intracellular bacterium Chlamydia
    • Hybiske, K., and R. Stephens. 2007. Mechanisms of host cell exit by the intracellular bacterium Chlamydia. Proc. Natl. Acad. Sci. USA 104:11430-11435.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11430-11435
    • Hybiske, K.1    Stephens, R.2
  • 22
    • 35648949958 scopus 로고    scopus 로고
    • Chlamydophila pneumoniae PknD exhibits dual amino acid specificity and phosphorylates Cpn0712, a putative type III secretion YscD homolog
    • Johnson, D., and J. Mahony. 2007. Chlamydophila pneumoniae PknD exhibits dual amino acid specificity and phosphorylates Cpn0712, a putative type III secretion YscD homolog. J. Bacteriol. 189:7549-7555.
    • (2007) J. Bacteriol , vol.189 , pp. 7549-7555
    • Johnson, D.1    Mahony, J.2
  • 23
    • 41949121055 scopus 로고    scopus 로고
    • Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type III secretion proteins
    • Johnson, D., C. Stone, and J. Mahony. 2008. Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type III secretion proteins. J. Bacteriol. 190:2972-2980.
    • (2008) J. Bacteriol , vol.190 , pp. 2972-2980
    • Johnson, D.1    Stone, C.2    Mahony, J.3
  • 24
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet, L., C. Agrain, P. Broz, and G. Cornelis. 2003. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302:1757-1760.
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.4
  • 25
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., N. Dautin, and D. Ladant. 2005. Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 187:2233-2243.
    • (2005) J. Bacteriol , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 26
    • 42949126864 scopus 로고    scopus 로고
    • Chlamydial entry involves TARP binding of guanine nucleotide exchange factors
    • Lane, B., C. Mutchler, S. Khodor, S. Grieshaber, and R. Carabeo. 2008. Chlamydial entry involves TARP binding of guanine nucleotide exchange factors. PLoS Pathog. 4:1-11.
    • (2008) PLoS Pathog , vol.4 , pp. 1-11
    • Lane, B.1    Mutchler, C.2    Khodor, S.3    Grieshaber, S.4    Carabeo, R.5
  • 27
    • 11244317087 scopus 로고    scopus 로고
    • Expression and localization of type III secretion-related proteins of Chlamydia pneumoniae
    • Lugert, R., M. Kuhns, T. Polch, and U. Gross. 2004. Expression and localization of type III secretion-related proteins of Chlamydia pneumoniae. Med. Microbiol. Immunol. 193:163-171.
    • (2004) Med. Microbiol. Immunol , vol.193 , pp. 163-171
    • Lugert, R.1    Kuhns, M.2    Polch, T.3    Gross, U.4
  • 28
    • 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 ATPase activity
    • Minamino, T., and M. Macnab. 2000. FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits ATPase activity. Mol. Microbiol. 37:1494-1503.
    • (2000) Mol. Microbiol , vol.37 , pp. 1494-1503
    • Minamino, T.1    Macnab, M.2
  • 29
    • 0025979037 scopus 로고
    • Interaction of chlamydiae and host cells in vitro
    • Moulder, J. 1991. Interaction of chlamydiae and host cells in vitro. Microbiol. Rev. 55:143-190.
    • (1991) Microbiol. Rev , vol.55 , pp. 143-190
    • Moulder, J.1
  • 31
    • 33645519210 scopus 로고    scopus 로고
    • Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the F0F1 and vacuolar ATPases
    • Pallen, M., C. Bailey, and S. Beatson. 2006. Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the F0F1 and vacuolar ATPases. Protein Sci. 15:935-940.
    • (2006) Protein Sci , vol.15 , pp. 935-940
    • Pallen, M.1    Bailey, C.2    Beatson, S.3
  • 33
    • 0038507200 scopus 로고    scopus 로고
    • Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization
    • Pozidis, C., A. Chalkiadaki, A. Gomez-Serrano, H. Stahlberg, I. Brown, A. Tampakaki, et al. 2003. Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization. J. Biol. Chem. 278:25816-25824.
    • (2003) J. Biol. Chem , vol.278 , pp. 25816-25824
    • Pozidis, C.1    Chalkiadaki, A.2    Gomez-Serrano, A.3    Stahlberg, H.4    Brown, I.5    Tampakaki, A.6
  • 34
    • 0035065113 scopus 로고    scopus 로고
    • Mammalian 14-3-3beta associates with the Chlamydia trachomatis inclusion membrane via its interaction with IncG
    • Scidmore, M., and T. Hackstadt. 2001. Mammalian 14-3-3beta associates with the Chlamydia trachomatis inclusion membrane via its interaction with IncG. Mol. Microbiol. 39:1638-1650.
    • (2001) Mol. Microbiol , vol.39 , pp. 1638-1650
    • Scidmore, M.1    Hackstadt, T.2
  • 35
    • 33750809905 scopus 로고    scopus 로고
    • Secretion signal recognition by YscN, the Yersinia type III secretion ATPase
    • Sorg, J., B. Blaylock, and O. Schneewind. 2006. Secretion signal recognition by YscN, the Yersinia type III secretion ATPase. Proc. Natl. Acad. Sci. USA 103:16490-16495.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16490-16495
    • Sorg, J.1    Blaylock, B.2    Schneewind, O.3
  • 37
    • 1542334775 scopus 로고    scopus 로고
    • Activation of Raf/Mek/Erk/cPLA2 signaling pathway is essential for chlamydial acquisition of host glycerophospholipids
    • Su, H., F. McClarty, G. Dong, Z. Hatch, K. Pan, and G. Zhong. 2004. Activation of Raf/Mek/Erk/cPLA2 signaling pathway is essential for chlamydial acquisition of host glycerophospholipids. J. Biol. Chem. 279:9409-9416.
    • (2004) J. Biol. Chem , vol.279 , pp. 9409-9416
    • Su, H.1    McClarty, F.2    Dong, G.3    Hatch, Z.4    Pan, K.5    Zhong, G.6
  • 38
    • 4444254395 scopus 로고    scopus 로고
    • Analysis of Chlamydia caviae entry sites and involvement of Cdc42 and Rac activity
    • Subtil, A., B. Wyplosz, M. Balana, and A. Dautry-Varsat. 2004. Analysis of Chlamydia caviae entry sites and involvement of Cdc42 and Rac activity. J. Cell Sci. 117:3923-3933.
    • (2004) J. Cell Sci , vol.117 , pp. 3923-3933
    • Subtil, A.1    Wyplosz, B.2    Balana, M.3    Dautry-Varsat, A.4
  • 39
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
    • Thomas, J., G. Stafford, and C. Hughes. 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.2    Hughes, C.3
  • 40
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S., A. Allaoui, P. Wattiau, and G. Cornelis. 1994. YscN, the putative energizer of the Yersinia Yop secretion machinery. J. Bacteriol. 176:1561-1569.
    • (1994) J. Bacteriol , vol.176 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.4
  • 41
    • 33846941536 scopus 로고    scopus 로고
    • Structural analysis of a prototypical ATPase from the type III secretion system
    • Zarivach, R., M. Vuckovic, W. Deng, B. Finlay, and N. Strynadka. 2007. Structural analysis of a prototypical ATPase from the type III secretion system. Nat. Struct. Mol. Biol. 14:131-137.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 131-137
    • Zarivach, R.1    Vuckovic, M.2    Deng, W.3    Finlay, B.4    Strynadka, N.5


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