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Volumn 67, Issue 6, 2008, Pages 1384-1401

The heat-shock protein ClpB of Francisella tularensis is involved in stress tolerance and is required for multiplication in target organs of infected mice

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN CLPB; LIVE VACCINE; UNCLASSIFIED DRUG;

EID: 39849093588     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06139.x     Document Type: Article
Times cited : (80)

References (72)
  • 1
    • 0031910620 scopus 로고    scopus 로고
    • Construction and characterization of a Helicobacter pylori clpB mutant and role of the gene in the stress response
    • Allan, E., Mullany, P., and Tabaqchali, S. (1998) Construction and characterization of a Helicobacter pylori clpB mutant and role of the gene in the stress response. J Bacteriol 180: 426–429.
    • (1998) J Bacteriol , vol.180 , pp. 426-429
    • Allan, E.1    Mullany, P.2    Tabaqchali, S.3
  • 2
    • 33845508218 scopus 로고    scopus 로고
    • Identification of MglA‐regulated genes reveals novel virulence factors in Francisella tularensis
    • Brotcke, A., Weiss, D.S., Kim, C.C., Chain, P., Malfatti, S., Garcia, E., and Monack, D.M. (2006) Identification of MglA‐regulated genes reveals novel virulence factors in Francisella tularensis. Infect Immun 74: 6642–6655.
    • (2006) Infect Immun , vol.74 , pp. 6642-6655
    • Brotcke, A.1    Weiss, D.S.2    Kim, C.C.3    Chain, P.4    Malfatti, S.5    Garcia, E.6    Monack, D.M.7
  • 3
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin‐like protein
    • Bryk, R., Lima, C.D., Erdjument‐Bromage, H., Tempst, P., and Nathan, C. (2002) Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin‐like protein. Science 295: 1073–1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument‐Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 4
    • 0037635296 scopus 로고    scopus 로고
    • Selection of small‐colony variants of Salmonella enterica serovar typhimurium in nonphagocytic eucaryotic cells
    • Cano, D.A., Pucciarelli, M.G., Martinez‐Moya, M., Casadesus, J., and Garcia‐del Portillo, F. (2003) Selection of small‐colony variants of Salmonella enterica serovar typhimurium in nonphagocytic eucaryotic cells. Infect Immun 71: 3690–3698.
    • (2003) Infect Immun , vol.71 , pp. 3690-3698
    • Cano, D.A.1    Pucciarelli, M.G.2    Martinez‐Moya, M.3    Casadesus, J.4    Garcia‐del Portillo, F.5
  • 5
    • 1142298585 scopus 로고    scopus 로고
    • clpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance
    • Chastanet, A., Derre, I., Nair, S., and Msadek, T. (2004) clpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance. J Bacteriol 186: 1165–1174.
    • (2004) J Bacteriol , vol.186 , pp. 1165-1174
    • Chastanet, A.1    Derre, I.2    Nair, S.3    Msadek, T.4
  • 6
    • 0028008788 scopus 로고
    • Fate of Listeria monocytogenes in murine macrophages: evidence for simultaneous killing and survival of intracellular bacteria
    • De Chastellier, C., and Berche, P. (1994) Fate of Listeria monocytogenes in murine macrophages: evidence for simultaneous killing and survival of intracellular bacteria. Infect Immun 62: 543–553.
    • (1994) Infect Immun , vol.62 , pp. 543-553
    • De Chastellier, C.1    Berche, P.2
  • 8
    • 2542552050 scopus 로고    scopus 로고
    • Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages
    • Clemens, D.L., Lee, B.Y., and Horwitz, M.A. (2004) Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages. Infect Immun 72: 3204–3217.
    • (2004) Infect Immun , vol.72 , pp. 3204-3217
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 10
    • 14644386907 scopus 로고    scopus 로고
    • A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPalpha) conjugative machineries and their cognate Escherichia coli host strains
    • Demarre, G., Guerout, A.M., Matsumoto‐Mashimo, C., Rowe‐Magnus, D.A., Marliere, P., and Mazel, D. (2005) A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPalpha) conjugative machineries and their cognate Escherichia coli host strains. Res Microbiol 156: 245–255.
    • (2005) Res Microbiol , vol.156 , pp. 245-255
    • Demarre, G.1    Guerout, A.M.2    Matsumoto‐Mashimo, C.3    Rowe‐Magnus, D.A.4    Marliere, P.5    Mazel, D.6
  • 11
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition, it all depends on their partner in crime
    • Dougan, D.A., Mogk, A., Zeth, K., Turgay, K., and Bukau, B. (2002) AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett 529: 6–10.
    • (2002) FEBS Lett , vol.529 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 12
    • 34547455220 scopus 로고    scopus 로고
    • Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system
    • Doyle, S.M., Hoskins, J.R., and Wickner, S. (2007) Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system. Proc Natl Acad Sci USA 104: 11138–11144.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11138-11144
    • Doyle, S.M.1    Hoskins, J.R.2    Wickner, S.3
  • 13
    • 0029063839 scopus 로고
    • Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family
    • Dramsi, S., Biswas, I., Maguin, E., Braun, L., Mastroeni, P., and Cossart, P. (1995) Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family. Mol Microbiol 16: 251–261.
    • (1995) Mol Microbiol , vol.16 , pp. 251-261
    • Dramsi, S.1    Biswas, I.2    Maguin, E.3    Braun, L.4    Mastroeni, P.5    Cossart, P.6
  • 14
    • 0035093653 scopus 로고    scopus 로고
    • Characterization of Brucella suis clpB and clpAB mutants and participation of the genes in stress responses
    • Ekaza, E., Teyssier, J., Ouahrani‐Bettache, S., Liautard, J.P., and Kohler, S. (2001) Characterization of Brucella suis clpB and clpAB mutants and participation of the genes in stress responses. J Bacteriol 183: 2677–2681.
    • (2001) J Bacteriol , vol.183 , pp. 2677-2681
    • Ekaza, E.1    Teyssier, J.2    Ouahrani‐Bettache, S.3    Liautard, J.P.4    Kohler, S.5
  • 15
    • 0028120804 scopus 로고
    • Increased synthesis of DnaK, GroEL, and GroES homologs by Francisella tularensis LVS in response to heat and hydrogen peroxide
    • Ericsson, M., Tarnvik, A., Kuoppa, K., Sandstrom, G., and Sjostedt, A. (1994) Increased synthesis of DnaK, GroEL, and GroES homologs by Francisella tularensis LVS in response to heat and hydrogen peroxide. Infect Immun 62: 178–183.
    • (1994) Infect Immun , vol.62 , pp. 178-183
    • Ericsson, M.1    Tarnvik, A.2    Kuoppa, K.3    Sandstrom, G.4    Sjostedt, A.5
  • 16
    • 0030987050 scopus 로고    scopus 로고
    • Characterization of the nucleotide sequence of the groE operon encoding heat shock proteins chaperone‐60 and ‐10 of Francisella tularensis and determination of the T‐cell response to the proteins in individuals vaccinated with F. tularensis
    • Ericsson, M., Golovliov, I., Sandstrom, G., Tarnvik, A., and Sjostedt, A. (1997) Characterization of the nucleotide sequence of the groE operon encoding heat shock proteins chaperone‐60 and ‐10 of Francisella tularensis and determination of the T‐cell response to the proteins in individuals vaccinated with F. tularensis. Infect Immun 65: 1824–1829.
    • (1997) Infect Immun , vol.65 , pp. 1824-1829
    • Ericsson, M.1    Golovliov, I.2    Sandstrom, G.3    Tarnvik, A.4    Sjostedt, A.5
  • 18
    • 0028953912 scopus 로고
    • Growth of Francisella tularensis LVS in macrophages: the acidic intracellular compartment provides essential iron required for growth
    • Fortier, A.H., Leiby, D.A., Narayanan, R.B., Asafoadjei, E., Crawford, R.M., Nacy, C.A., and Meltzer, M.S. (1995) Growth of Francisella tularensis LVS in macrophages: the acidic intracellular compartment provides essential iron required for growth. Infect Immun 63: 1478–1483.
    • (1995) Infect Immun , vol.63 , pp. 1478-1483
    • Fortier, A.H.1    Leiby, D.A.2    Narayanan, R.B.3    Asafoadjei, E.4    Crawford, R.M.5    Nacy, C.A.6    Meltzer, M.S.7
  • 19
    • 9644274213 scopus 로고    scopus 로고
    • Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus
    • Frees, D., Chastanet, A., Qazi, S., Sorensen, K., Hill, P., Msadek, T., and Ingmer, H. (2004) Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus. Mol Microbiol 54: 1445–1462.
    • (2004) Mol Microbiol , vol.54 , pp. 1445-1462
    • Frees, D.1    Chastanet, A.2    Qazi, S.3    Sorensen, K.4    Hill, P.5    Msadek, T.6    Ingmer, H.7
  • 20
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover, J.R., and Lindquist, S. (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73–82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 21
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff, P., Mogk, A., Zvi, A.P., Tomoyasu, T., and Bukau, B. (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 96: 13732–13737.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 23
    • 0037167471 scopus 로고    scopus 로고
    • The identification of five genetic loci of Francisella novicida associated with intracellular growth
    • Gray, C.G., Cowley, S.C., Cheung, K.K., and Nano, F.E. (2002) The identification of five genetic loci of Francisella novicida associated with intracellular growth. FEMS Microbiol Lett 215: 53–56.
    • (2002) FEMS Microbiol Lett , vol.215 , pp. 53-56
    • Gray, C.G.1    Cowley, S.C.2    Cheung, K.K.3    Nano, F.E.4
  • 24
    • 0001241680 scopus 로고    scopus 로고
    • Function and regulation of the heat shock proteins, in: Escherichia coli and Salmonella: Cellular and Molecular Biology
    • Gross, C.A. (1996) Function and regulation of the heat shock proteins. In: Escherichia coli and Salmonella: Cellular and Molecular Biology. Neidhardt, F.C. (ed.). Washington, DC: American Society for Microbiology Press, pp. 1382–1399.
    • (1996) , pp. 1382-1399
    • Gross, C.A.1
  • 25
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • Gruber, T.M., and Gross, C.A. (2003) Multiple sigma subunits and the partitioning of bacterial transcription space. Annu Rev Microbiol 57: 441–466.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 26
    • 33846231395 scopus 로고    scopus 로고
    • M domains couple the ClpB threading motor with the DnaK chaperone activity
    • Haslberger, T., Weibezahn, J., Zahn, R., Lee, S., Tsai, F.T., Bukau, B., and Mogk, A. (2007) M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell 25: 247–260.
    • (2007) Mol Cell , vol.25 , pp. 247-260
    • Haslberger, T.1    Weibezahn, J.2    Zahn, R.3    Lee, S.4    Tsai, F.T.5    Bukau, B.6    Mogk, A.7
  • 27
    • 18144424963 scopus 로고    scopus 로고
    • Proteomic analysis of anti‐Francisella tularensis LVS antibody response in murine model of tularemia
    • Havlasova, J., Hernychova, L., Brychta, M., Hubalek, M., Lenco, J., Larsson, P., et al. (2005) Proteomic analysis of anti‐ Francisella tularensis LVS antibody response in murine model of tularemia. Proteomics 5: 2090–2103.
    • (2005) Proteomics , vol.5 , pp. 2090-2103
    • Havlasova, J.1    Hernychova, L.2    Brychta, M.3    Hubalek, M.4    Lenco, J.5    Larsson, P.6
  • 28
    • 0038110099 scopus 로고    scopus 로고
    • Aerobic growth deficient Haemophilus influenzae mutants are non‐virulent: implications on metabolism
    • Herbert, M., Kraiss, A., Hilpert, A.K., Schlor, S., and Reidl, J. (2003) Aerobic growth deficient Haemophilus influenzae mutants are non‐virulent: implications on metabolism. Int J Med Microbiol 293: 145–152.
    • (2003) Int J Med Microbiol , vol.293 , pp. 145-152
    • Herbert, M.1    Kraiss, A.2    Hilpert, A.K.3    Schlor, S.4    Reidl, J.5
  • 29
    • 0024185105 scopus 로고
    • ‘Catalysts’ for polyacrylamide gel polymerization and detection of proteins by silver staining
    • Hochstrasser, D.F., and Merril, C.R. (1988) ‘Catalysts’ for polyacrylamide gel polymerization and detection of proteins by silver staining. Appl Theor Electrophor 1: 35–40.
    • (1988) Appl Theor Electrophor , vol.1 , pp. 35-40
    • Hochstrasser, D.F.1    Merril, C.R.2
  • 30
    • 31844440317 scopus 로고    scopus 로고
    • Identification of a virulence‐associated determinant, dihydrolipoamide dehydrogenase (lpd), in Mycoplasma gallisepticum through in vivo screening of transposon mutants
    • Hudson, P., Gorton, T.S., Papazisi, L., Cecchini, K., Frasca, S., Jr, and Geary, S.J. (2006) Identification of a virulence‐associated determinant, dihydrolipoamide dehydrogenase (lpd), in Mycoplasma gallisepticum through in vivo screening of transposon mutants. Infect Immun 74: 931–939.
    • (2006) Infect Immun , vol.74 , pp. 931-939
    • Hudson, P.1    Gorton, T.S.2    Papazisi, L.3    Cecchini, K.4    Frasca, S.5    Geary, S.J.6
  • 31
    • 33846700954 scopus 로고    scopus 로고
    • Identification of immunoreactive antigens in membrane proteins enriched fraction from Francisella tularensis LVS
    • Janovska, S., Pavkova, I., Hubalek, M., Lenco, J., Macela, A., and Stulik, J. (2007) Identification of immunoreactive antigens in membrane proteins enriched fraction from Francisella tularensis LVS. Immunol Lett 108: 151–159.
    • (2007) Immunol Lett , vol.108 , pp. 151-159
    • Janovska, S.1    Pavkova, I.2    Hubalek, M.3    Lenco, J.4    Macela, A.5    Stulik, J.6
  • 32
    • 0035960731 scopus 로고    scopus 로고
    • Construction of a reporter plasmid for screening in vivo promoter activity in Francisella tularensis
    • Kuoppa, K., Forsberg, A., and Norqvist, A. (2001) Construction of a reporter plasmid for screening in vivo promoter activity in Francisella tularensis. FEMS Microbiol Lett 205: 77–81.
    • (2001) FEMS Microbiol Lett , vol.205 , pp. 77-81
    • Kuoppa, K.1    Forsberg, A.2    Norqvist, A.3
  • 33
    • 1642447175 scopus 로고    scopus 로고
    • MglA regulates transcription of virulence factors necessary for Francisella tularensis intraamoebae and intramacrophage survival
    • Lauriano, C.M., Barker, J.R., Yoon, S.S., Nano, F.E., Arulanandam, B.P., Hassett, D.J., and Klose, K.E. (2004) MglA regulates transcription of virulence factors necessary for Francisella tularensis intraamoebae and intramacrophage survival. Proc Natl Acad Sci USA 101: 4246–4249.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4246-4249
    • Lauriano, C.M.1    Barker, J.R.2    Yoon, S.S.3    Nano, F.E.4    Arulanandam, B.P.5    Hassett, D.J.6    Klose, K.E.7
  • 34
    • 18144420399 scopus 로고    scopus 로고
    • Insights into the oxidative stress response in Francisella tularensis LVS and its mutant DeltaiglC1+2 by proteomics analysis
    • Lenco, J., Pavkova, I., Hubalek, M., and Stulik, J. (2005) Insights into the oxidative stress response in Francisella tularensis LVS and its mutant DeltaiglC1+2 by proteomics analysis. FEMS Microbiol Lett 246: 47–54.
    • (2005) FEMS Microbiol Lett , vol.246 , pp. 47-54
    • Lenco, J.1    Pavkova, I.2    Hubalek, M.3    Stulik, J.4
  • 35
    • 9244229561 scopus 로고    scopus 로고
    • Distinct roles of reactive nitrogen and oxygen species to control infection with the facultative intracellular bacterium Francisella tularensis
    • Lindgren, H., Stenmark, S., Chen, W., Tarnvik, A., and Sjostedt, A. (2004) Distinct roles of reactive nitrogen and oxygen species to control infection with the facultative intracellular bacterium Francisella tularensis. Infect Immun 72: 7172–7182.
    • (2004) Infect Immun , vol.72 , pp. 7172-7182
    • Lindgren, H.1    Stenmark, S.2    Chen, W.3    Tarnvik, A.4    Sjostedt, A.5
  • 36
    • 18044362697 scopus 로고    scopus 로고
    • The contribution of reactive nitrogen and oxygen species to the killing of Francisella tularensis LVS by murine macrophages
    • Lindgren, H., Stenman, L., Tarnvik, A., and Sjostedt, A. (2005) The contribution of reactive nitrogen and oxygen species to the killing of Francisella tularensis LVS by murine macrophages. Microbes Infect 7: 467–475.
    • (2005) Microbes Infect , vol.7 , pp. 467-475
    • Lindgren, H.1    Stenman, L.2    Tarnvik, A.3    Sjostedt, A.4
  • 37
    • 33847716729 scopus 로고    scopus 로고
    • The resistance of Francisella strains against reactive nitrogen and oxygen species with special reference to the role of KatG
    • Lindgren, H., Shen, H., Zingmark, C., Golovliov, I., Conlan, W., and Sjostedt, A. (2007) The resistance of Francisella strains against reactive nitrogen and oxygen species with special reference to the role of KatG. Infect Immun 75: 1303–1309.
    • (2007) Infect Immun , vol.75 , pp. 1303-1309
    • Lindgren, H.1    Shen, H.2    Zingmark, C.3    Golovliov, I.4    Conlan, W.5    Sjostedt, A.6
  • 38
    • 33644941364 scopus 로고    scopus 로고
    • In vivo Himar1‐based transposon mutagenesis of Francisella tularensis
    • Maier, T.M., Pechous, R., Casey, M., Zahrt, T.C., and Frank, D.W. (2006) In vivo Himar1‐based transposon mutagenesis of Francisella tularensis. Appl Environ Microbiol 72: 1878–1885.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1878-1885
    • Maier, T.M.1    Pechous, R.2    Casey, M.3    Zahrt, T.C.4    Frank, D.W.5
  • 39
    • 1242283848 scopus 로고    scopus 로고
    • Protein binding and disruption by Clp/Hsp100 chaperones
    • Maurizi, M.R., and Xia, D. (2004) Protein binding and disruption by Clp/Hsp100 chaperones. Structure 12: 175–183.
    • (2004) Structure , vol.12 , pp. 175-183
    • Maurizi, M.R.1    Xia, D.2
  • 40
    • 34447281114 scopus 로고    scopus 로고
    • Identification of an orphan response regulator required for the virulence of Francisella spp. and transcription of pathogenicity island genes
    • Mohapatra, N.P., Soni, S., Bell, B.L., Warren, R., Ernst, R.K., Muszynski, A., et al. (2007) Identification of an orphan response regulator required for the virulence of Francisella spp. and transcription of pathogenicity island genes. Infect Immun 75: 3305–3314.
    • (2007) Infect Immun , vol.75 , pp. 3305-3314
    • Mohapatra, N.P.1    Soni, S.2    Bell, B.L.3    Warren, R.4    Ernst, R.K.5    Muszynski, A.6
  • 41
    • 18844454755 scopus 로고    scopus 로고
    • In vivo induced clpB1 gene of Vibrio cholerae is involved in different stress responses and affects in vivo cholera toxin production
    • Nag, S., Das, S., and Chaudhuri, K. (2005) In vivo induced clpB1 gene of Vibrio cholerae is involved in different stress responses and affects in vivo cholera toxin production. Biochem Biophys Res Commun 331: 1365–1373.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 1365-1373
    • Nag, S.1    Das, S.2    Chaudhuri, K.3
  • 42
    • 0032920682 scopus 로고    scopus 로고
    • ClpE, a novel member of the HSP100 family, is involved in cell division and virulence of Listeria monocytogenes
    • Nair, S., Frehel, C., Nguyen, L., Escuyer, V., and Berche, P. (1999) ClpE, a novel member of the HSP100 family, is involved in cell division and virulence of Listeria monocytogenes. Mol Microbiol 31: 185–196.
    • (1999) Mol Microbiol , vol.31 , pp. 185-196
    • Nair, S.1    Frehel, C.2    Nguyen, L.3    Escuyer, V.4    Berche, P.5
  • 43
    • 4544341163 scopus 로고    scopus 로고
    • A Francisella tularensis pathogenicity island required for intramacrophage growth
    • Nano, F.E., Zhang, N., Cowley, S.C., Klose, K.E., Cheung, K.K., Roberts, M.J., et al. (2004) A Francisella tularensis pathogenicity island required for intramacrophage growth. J Bacteriol 186: 6430–6436.
    • (2004) J Bacteriol , vol.186 , pp. 6430-6436
    • Nano, F.E.1    Zhang, N.2    Cowley, S.C.3    Klose, K.E.4    Cheung, K.K.5    Roberts, M.J.6
  • 44
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: a class of chaperone‐like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A.F., Aravind, L., Spouge, J.L., and Koonin, E.V. (1999) AAA+: a class of chaperone‐like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9: 27–43.
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 45
    • 33745618956 scopus 로고    scopus 로고
    • Regulon and promoter analysis of the E. coli heat‐shock factor, sigma32, reveals a multifaceted cellular response to heat stress
    • Nonaka, G., Blankschien, M., Herman, C., Gross, C.A., and Rhodius, V.A. (2006) Regulon and promoter analysis of the E. coli heat‐shock factor, sigma32, reveals a multifaceted cellular response to heat stress. Genes Dev 20: 1776–1789.
    • (2006) Genes Dev , vol.20 , pp. 1776-1789
    • Nonaka, G.1    Blankschien, M.2    Herman, C.3    Gross, C.A.4    Rhodius, V.A.5
  • 46
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions
    • Perham, R.N. (2000) Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 69: 961–1004.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 47
    • 33846024366 scopus 로고    scopus 로고
    • Role of the wbt locus of Francisella tularensis in lipopolysaccharide O‐antigen biogenesis and pathogenicity
    • Raynaud, C., Meibom, K.L., Lety, M.A., Dubail, I., Candela, T., Frapy, E., and Charbit, A. (2007) Role of the wbt locus of Francisella tularensis in lipopolysaccharide O‐antigen biogenesis and pathogenicity. Infect Immun 75: 536–541.
    • (2007) Infect Immun , vol.75 , pp. 536-541
    • Raynaud, C.1    Meibom, K.L.2    Lety, M.A.3    Dubail, I.4    Candela, T.5    Frapy, E.6    Charbit, A.7
  • 49
    • 33645094973 scopus 로고
    • [A graphic probit method for the calculation of LD50 and relative toxicity.]
    • Roth, Z. (1961) [A graphic probit method for the calculation of LD50 and relative toxicity.] Cesk Fysiol 10: 408–422.
    • (1961) Cesk Fysiol , vol.10 , pp. 408-422
    • Roth, Z.1
  • 50
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez, Y., and Lindquist, S.L. (1990) HSP104 required for induced thermotolerance. Science 248: 1112–1115.
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 51
    • 34548411393 scopus 로고    scopus 로고
    • A Francisella tularensis pathogenicity island protein essential for bacterial proliferation within the host cell cytosol
    • Santic, M., Molmeret, M., Barker, J.R., Klose, K.E., Dekanic, A., Doric, M., and Kwaik, Y.A. (2007) A Francisella tularensis pathogenicity island protein essential for bacterial proliferation within the host cell cytosol. Cell Microbiol 9: 2391–2403.
    • (2007) Cell Microbiol , vol.9 , pp. 2391-2403
    • Santic, M.1    Molmeret, M.2    Barker, J.R.3    Klose, K.E.4    Dekanic, A.5    Doric, M.6    Kwaik, Y.A.7
  • 52
    • 5344269437 scopus 로고    scopus 로고
    • Sculpting the proteome with AAA(+) proteases and disassembly machines
    • Sauer, R.T., Bolon, D.N., Burton, B.M., Burton, R.E., Flynn, J.M., Grant, R.A., et al. (2004) Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119: 9–18.
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1    Bolon, D.N.2    Burton, B.M.3    Burton, R.E.4    Flynn, J.M.5    Grant, R.A.6
  • 53
    • 0030219939 scopus 로고    scopus 로고
    • HSP100/Clp proteins: a common mechanism explains diverse functions
    • Schirmer, E.C., Glover, J.R., Singer, M.A., and Lindquist, S. (1996) HSP100/Clp proteins: a common mechanism explains diverse functions. Trends Biochem Sci 21: 289–296.
    • (1996) Trends Biochem Sci , vol.21 , pp. 289-296
    • Schirmer, E.C.1    Glover, J.R.2    Singer, M.A.3    Lindquist, S.4
  • 54
    • 28244467883 scopus 로고    scopus 로고
    • ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria
    • Schlieker, C., Zentgraf, H., Dersch, P., and 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
  • 55
    • 0043142536 scopus 로고    scopus 로고
    • Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment
    • Schnappinger, D., Ehrt, S., Voskuil, M.I., Liu, Y., Mangan, J.A., Monahan, I.M., et al. (2003) Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment. J Exp Med 198: 693–704.
    • (2003) J Exp Med , vol.198 , pp. 693-704
    • Schnappinger, D.1    Ehrt, S.2    Voskuil, M.I.3    Liu, Y.4    Mangan, J.A.5    Monahan, I.M.6
  • 56
    • 34248379117 scopus 로고    scopus 로고
    • A defined O‐antigen polysaccharide mutant of Francisella tularensis live vaccine strain has attenuated virulence while retaining its protective capacity
    • Sebastian, S., Dillon, S.T., Lynch, J.G., Blalock, L.T., Balon, E., Lee, K.T., et al. (2007) A defined O‐antigen polysaccharide mutant of Francisella tularensis live vaccine strain has attenuated virulence while retaining its protective capacity. Infect Immun 75: 2591–2602.
    • (2007) Infect Immun , vol.75 , pp. 2591-2602
    • Sebastian, S.1    Dillon, S.T.2    Lynch, J.G.3    Blalock, L.T.4    Balon, E.5    Lee, K.T.6
  • 57
    • 22144472269 scopus 로고    scopus 로고
    • Cells lacking ClpB display a prolonged shutoff phase of the heat shock response in Caulobacter crescentus
    • Simao, R.C., Susin, M.F., Alvarez‐Martinez, C.E., and Gomes, S.L. (2005) Cells lacking ClpB display a prolonged shutoff phase of the heat shock response in Caulobacter crescentus. Mol Microbiol 57: 592–603.
    • (2005) Mol Microbiol , vol.57 , pp. 592-603
    • Simao, R.C.1    Susin, M.F.2    Alvarez‐Martinez, C.E.3    Gomes, S.L.4
  • 58
    • 32244446027 scopus 로고    scopus 로고
    • Intracellular survival mechanisms of Francisella tularensis, a stealth pathogen
    • Sjostedt, A. (2006) Intracellular survival mechanisms of Francisella tularensis, a stealth pathogen. Microbes Infect 8: 561–567.
    • (2006) Microbes Infect , vol.8 , pp. 561-567
    • Sjostedt, A.1
  • 59
    • 33846241675 scopus 로고    scopus 로고
    • Global gene expression and phenotypic analysis of a Vibrio cholerae rpoH deletion mutant
    • Slamti, L., Livny, J., and Waldor, M.K. (2007) Global gene expression and phenotypic analysis of a Vibrio cholerae rpoH deletion mutant. J Bacteriol 189: 351–362.
    • (2007) J Bacteriol , vol.189 , pp. 351-362
    • Slamti, L.1    Livny, J.2    Waldor, M.K.3
  • 60
    • 0036228111 scopus 로고    scopus 로고
    • Characterization of the dihydrolipoamide dehydrogenase from Streptococcus pneumoniae and its role in pneumococcal infection
    • Smith, A.W., Roche, H., Trombe, M.C., Briles, D.E., and Hakansson, A. (2002) Characterization of the dihydrolipoamide dehydrogenase from Streptococcus pneumoniae and its role in pneumococcal infection. Mol Microbiol 44: 431–448.
    • (2002) Mol Microbiol , vol.44 , pp. 431-448
    • Smith, A.W.1    Roche, H.2    Trombe, M.C.3    Briles, D.E.4    Hakansson, A.5
  • 61
    • 0026571094 scopus 로고
    • The Clp proteins: proteolysis regulators or molecular chaperones?
    • Squires, C., and Squires, C.L. (1992) The Clp proteins: proteolysis regulators or molecular chaperones? J Bacteriol 174: 1081–1085.
    • (1992) J Bacteriol , vol.174 , pp. 1081-1085
    • Squires, C.1    Squires, C.L.2
  • 62
    • 34249868441 scopus 로고    scopus 로고
    • Genome‐wide identification of Francisella tularensis virulence determinants
    • Su, J., Yang, J., Zhao, D., Kawula, T.H., Banas, J.A., and Zhang, J.‐R. (2007) Genome‐wide identification of Francisella tularensis virulence determinants. Infect Immun 75: 3089–3101.
    • (2007) Infect Immun , vol.75 , pp. 3089-3101
    • Su, J.1    Yang, J.2    Zhao, D.3    Kawula, T.H.4    Banas, J.A.5    Zhang, J.‐R.6
  • 63
    • 33748028835 scopus 로고    scopus 로고
    • Attenuated Francisella novicida transposon mutants protect mice against wild‐type challenge
    • Tempel, R., Lai, X.H., Crosa, L., Kozlowicz, B., and Heffron, F. (2006) Attenuated Francisella novicida transposon mutants protect mice against wild‐type challenge. Infect Immun 74: 5095–5105.
    • (2006) Infect Immun , vol.74 , pp. 5095-5105
    • Tempel, R.1    Lai, X.H.2    Crosa, L.3    Kozlowicz, B.4    Heffron, F.5
  • 64
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG in vivo
    • Thomas, J.G., and Baneyx, F. (1998) Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG in vivo. J Bacteriol 180: 5165–5172.
    • (1998) J Bacteriol , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 65
    • 33845979136 scopus 로고    scopus 로고
    • The immunologically distinct O antigens from Francisella tularensis subspecies tularensis and Francisella novicida are both virulence determinants and protective antigens
    • Thomas, R.M., Titball, R.W., Oyston, P.C., Griffin, K., Waters, E., Hitchen, P.G., et al. (2007) The immunologically distinct O antigens from Francisella tularensis subspecies tularensis and Francisella novicida are both virulence determinants and protective antigens. Infect Immun 75: 371–378.
    • (2007) Infect Immun , vol.75 , pp. 371-378
    • Thomas, R.M.1    Titball, R.W.2    Oyston, P.C.3    Griffin, K.4    Waters, E.5    Hitchen, P.G.6
  • 66
    • 0242417000 scopus 로고    scopus 로고
    • Gene expression profiling of Helicobacter pylori reveals a growth‐phase‐dependent switch in virulence gene expression
    • Thompson, L.J., Merrell, D.S., Neilan, B.A., Mitchell, H., Lee, A., and Falkow, S. (2003) Gene expression profiling of Helicobacter pylori reveals a growth‐phase‐dependent switch in virulence gene expression. Infect Immun 71: 2643–2655.
    • (2003) Infect Immun , vol.71 , pp. 2643-2655
    • Thompson, L.J.1    Merrell, D.S.2    Neilan, B.A.3    Mitchell, H.4    Lee, A.5    Falkow, S.6
  • 67
    • 0031900977 scopus 로고    scopus 로고
    • Identification of Salmonella typhimurium genes required for colonization of the chicken alimentary tract and for virulence in newly hatched chicks
    • Turner, A.K., Lovell, M.A., Hulme, S.D., Zhang‐Barber, L., and Barrow, P.A. (1998) Identification of Salmonella typhimurium genes required for colonization of the chicken alimentary tract and for virulence in newly hatched chicks. Infect Immun 66: 2099–2106.
    • (1998) Infect Immun , vol.66 , pp. 2099-2106
    • Turner, A.K.1    Lovell, M.A.2    Hulme, S.D.3    Zhang‐Barber, L.4    Barrow, P.A.5
  • 68
    • 34247265920 scopus 로고    scopus 로고
    • Attenuated virulence of a Francisella mutant lacking the lipid A 4′‐phosphatase
    • Wang, X., Ribeiro, A.A., Guan, Z., Abraham, S.N., and Raetz, C.R.H. (2007) Attenuated virulence of a Francisella mutant lacking the lipid A 4′‐phosphatase. Proc Natl Acad Sci USA 104: 4136–4141.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4136-4141
    • Wang, X.1    Ribeiro, A.A.2    Guan, Z.3    Abraham, S.N.4    Raetz, C.R.H.5
  • 69
    • 8844251486 scopus 로고    scopus 로고
    • Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
    • Weibezahn, J., Tessarz, P., Schlieker, C., Zahn, R., Maglica, Z., Lee, S., et al. (2004) Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119: 653–665.
    • (2004) Cell , vol.119 , pp. 653-665
    • Weibezahn, J.1    Tessarz, P.2    Schlieker, C.3    Zahn, R.4    Maglica, Z.5    Lee, S.6
  • 70
    • 34347270217 scopus 로고    scopus 로고
    • In vivo negative selection screen identifies genes required for Francisella virulence
    • Weiss, D.S., Brotcke, A., Henry, T., Margolis, J.J., Chan, K., and Monack, D.M. (2007) In vivo negative selection screen identifies genes required for Francisella virulence. Proc Natl Acad Sci USA 104: 6037–6042.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 6037-6042
    • Weiss, D.S.1    Brotcke, A.2    Henry, T.3    Margolis, J.J.4    Chan, K.5    Monack, D.M.6
  • 71
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi‐chaperone system from Escherichia coli
    • Zolkiewski, M. (1999) ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi‐chaperone system from Escherichia coli. J Biol Chem 274: 28083–28086.
    • (1999) J Biol Chem , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1
  • 72
    • 33747058216 scopus 로고    scopus 로고
    • A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases
    • Zolkiewski, M. (2006) A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases. Mol Microbiol 61: 1094–1100.
    • (2006) Mol Microbiol , vol.61 , pp. 1094-1100
    • Zolkiewski, M.1


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