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Volumn 74, Issue 2, 2009, Pages 315-329

Role of DegP for two-partner secretion in Bordetella

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DEGP PROTEIN; HEMAGGLUTININ; UNCLASSIFIED DRUG;

EID: 70349922815     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06860.x     Document Type: Article
Times cited : (48)

References (58)
  • 1
    • 0036078538 scopus 로고    scopus 로고
    • Eighty-kilodalton N-terminal moiety of Bordetella pertussis filamentous hemagglutinin: Adherence, immunogenicity, and protective role
    • Alonso, S., Reveneau, N., Pethe, K. Locht, C. (2002) Eighty-kilodalton N-terminal moiety of Bordetella pertussis filamentous hemagglutinin: adherence, immunogenicity, and protective role. Infect Immun 70 : 4142 4147.
    • (2002) Infect Immun , vol.70 , pp. 4142-4147
    • Alonso, S.1    Reveneau, N.2    Pethe, K.3    Locht, C.4
  • 2
    • 0033818865 scopus 로고    scopus 로고
    • New virulence-activated and virulence-repressed genes identified by systematic gene inactivation and generation of transcriptional fusions in Bordetella pertussis
    • Antoine, R., Alonso, S., Raze, D., Coutte, L., Lesjean, S., Willery, E., et al. (2000) New virulence-activated and virulence-repressed genes identified by systematic gene inactivation and generation of transcriptional fusions in Bordetella pertussis. J Bacteriol 182 : 5902 5905.
    • (2000) J Bacteriol , vol.182 , pp. 5902-5905
    • Antoine, R.1    Alonso, S.2    Raze, D.3    Coutte, L.4    Lesjean, S.5    Willery, E.6
  • 4
    • 0037214416 scopus 로고    scopus 로고
    • Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture
    • CastilloKeller, M. Misra, R. (2003) Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture. J Bacteriol 185 : 148 154.
    • (2003) J Bacteriol , vol.185 , pp. 148-154
    • Castillokeller, M.1    Misra, R.2
  • 6
    • 1942437434 scopus 로고    scopus 로고
    • The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway
    • Clantin, B., Hodak, H., Willery, E., Locht, C., Jacob-Dubuisson, F. Villeret, V. (2004) The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway. Proc Natl Acad Sci USA 101 : 6194 6199.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6194-6199
    • Clantin, B.1    Hodak, H.2    Willery, E.3    Locht, C.4    Jacob-Dubuisson, F.5    Villeret, V.6
  • 7
    • 34548128883 scopus 로고    scopus 로고
    • Structure of the membrane protein FhaC: A member of the Omp85-TpsB transporter superfamily
    • Clantin, B., Delattre, A.S., Rucktooa, P., Saint, N., Meli, A.C., Locht, C., et al. (2007) Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily. Science 317 : 957 961.
    • (2007) Science , vol.317 , pp. 957-961
    • Clantin, B.1    Delattre, A.S.2    Rucktooa, P.3    Saint, N.4    Meli, A.C.5    Locht, C.6
  • 8
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition and cell fate
    • Clausen, T., Southan, C. Ehrmann, M. (2002) The HtrA family of proteases: implications for protein composition and cell fate. Mol Cell 10 : 443 455.
    • (2002) Mol Cell , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 9
    • 0035903666 scopus 로고    scopus 로고
    • Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway
    • Coutte, L., Antoine, R., Drobecq, H., Locht, C. Jacob-Dubuisson, F. (2001) Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway. EMBO J 20 : 5040 5048.
    • (2001) EMBO J , vol.20 , pp. 5040-5048
    • Coutte, L.1    Antoine, R.2    Drobecq, H.3    Locht, C.4    Jacob-Dubuisson, F.5
  • 10
    • 42449144218 scopus 로고    scopus 로고
    • Influence of the passenger domain of a model autotransporter on the properties of its translocator domain
    • De, E., Saint, N., Glinel, K., Meli, A.C., Levy, D. Jacob-Dubuisson, F. (2008) Influence of the passenger domain of a model autotransporter on the properties of its translocator domain. Mol Membr Biol 25 : 192 202.
    • (2008) Mol Membr Biol , vol.25 , pp. 192-202
    • De, E.1    Saint, N.2    Glinel, K.3    Meli, A.C.4    Levy, D.5    Jacob-Dubuisson, F.6
  • 11
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • DOI 10.1126/science.1127895
    • Dolezal, P., Likic, V., Tachezy, J. Lithgow, T. (2006) Evolution of the molecular machines for protein import into mitochondria. Science 313 : 314 318. (Pubitemid 44480948)
    • (2006) Science , vol.313 , Issue.5785 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 12
    • 0025311307 scopus 로고
    • Genetic characterization of Bordetella pertussis filamentous hemagglutinin: A protein processed from an unusually large precursor
    • Domenighini, M., Relman, D., Capiau, C., Falkow, S., Prugnola, A., Scarlato, V. Rappuoli, R. (1990) Genetic characterization of Bordetella pertussis filamentous hemagglutinin: a protein processed from an unusually large precursor. Mol Microbiol 4 : 787 800.
    • (1990) Mol Microbiol , vol.4 , pp. 787-800
    • Domenighini, M.1    Relman, D.2    Capiau, C.3    Falkow, S.4    Prugnola, A.5    Scarlato, V.6    Rappuoli, R.7
  • 13
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley, P., Charles, I.G., Fairweather, N.F. Isaacs, N.W. (1996) Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 381 : 90 92.
    • (1996) Nature , vol.381 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 14
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Fürste, J.P., Pansegrau, W., Frank, R., Blöcker, H., Scholz, P., Bagdasarian, M. Lanka, E. (1986) Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48 : 119 131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Fürste, J.P.1    Pansegrau, W.2    Frank, R.3    Blöcker, H.4    Scholz, P.5    Bagdasarian, M.6    Lanka, E.7
  • 15
    • 0034034907 scopus 로고    scopus 로고
    • Maturation and secretion of the non-typable Haemophilus influenzae HMW1 adhesin: Roles of the N-terminal and C-terminal domains
    • 3rd
    • Grass, S. St Geme, J.W., 3rd (2000) Maturation and secretion of the non-typable Haemophilus influenzae HMW1 adhesin: roles of the N-terminal and C-terminal domains. Mol Microbiol 36 : 55 67.
    • (2000) Mol Microbiol , vol.36 , pp. 55-67
    • Grass, S.1    St Geme, J.W.2
  • 16
    • 20944444077 scopus 로고    scopus 로고
    • Implications of the serine protease HtrA1 in amyloid precursor protein processing
    • Grau, S., Baldi, A., Bussani, R., Tian, X., Stefanescu, R., Przybylski, M., et al. (2005) Implications of the serine protease HtrA1 in amyloid precursor protein processing. Proc Natl Acad Sci USA 102 : 6021 6026.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6021-6026
    • Grau, S.1    Baldi, A.2    Bussani, R.3    Tian, X.4    Stefanescu, R.5    Przybylski, M.6
  • 17
    • 0031927529 scopus 로고    scopus 로고
    • Evidence that a globular conformation is not compatible with FhaC-mediated secretion of the Bordetella pertussis filamentous haemagglutinin
    • Guédin, S., Willery, E., Locht, C. Jacob-Dubuisson, F. (1998) Evidence that a globular conformation is not compatible with FhaC-mediated secretion of the Bordetella pertussis filamentous haemagglutinin. Mol Microbiol 29 : 763 774.
    • (1998) Mol Microbiol , vol.29 , pp. 763-774
    • Guédin, S.1    Willery, E.2    Locht, C.3    Jacob-Dubuisson, F.4
  • 18
    • 0034730655 scopus 로고    scopus 로고
    • Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin
    • Guédin, S., Willery, E., Tommassen, J., Fort, E., Drobecq, H., Locht, C. Jacob-Dubuisson, F. (2000) Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J Biol Chem 275 : 30202 30210.
    • (2000) J Biol Chem , vol.275 , pp. 30202-30210
    • Guédin, S.1    Willery, E.2    Tommassen, J.3    Fort, E.4    Drobecq, H.5    Locht, C.6    Jacob-Dubuisson, F.7
  • 19
    • 33748496461 scopus 로고    scopus 로고
    • Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate
    • Hodak, H., Clantin, B., Willery, E., Villeret, V., Locht, C. Jacob-Dubuisson, F. (2006) Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate. Mol Microbiol 61 : 368 382.
    • (2006) Mol Microbiol , vol.61 , pp. 368-382
    • Hodak, H.1    Clantin, B.2    Willery, E.3    Villeret, V.4    Locht, C.5    Jacob-Dubuisson, F.6
  • 20
    • 38349137103 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins
    • Hodak, H., Wohlkonig, A., Smet-Nocca, C., Drobecq, H., Wieruszeski, J.M., Senechal, M., et al. (2008) The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins. J Mol Biol 376 : 414 426.
    • (2008) J Mol Biol , vol.376 , pp. 414-426
    • Hodak, H.1    Wohlkonig, A.2    Smet-Nocca, C.3    Drobecq, H.4    Wieruszeski, J.M.5    Senechal, M.6
  • 21
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • Huth, J.R., Bewley, C.A., Jackson, B.M., Hinnebusch, A.G., Clore, G.M. Gronenborn, A.M. (1997) Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci 6 : 2359 2364.
    • (1997) Protein Sci , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 22
    • 0020505228 scopus 로고
    • Heptakis (2,6-O-dimethyl)beta-cyclodextrin: A novel growth stimulant for Bordetella pertussis phase i
    • Imaizumi, A., Suzuki, Y., Ono, S., Sato, Y. Sato, H. (1983) Heptakis (2,6-O-dimethyl)beta-cyclodextrin: a novel growth stimulant for Bordetella pertussis phase I. J Clin Microbiol 17 : 781 786.
    • (1983) J Clin Microbiol , vol.17 , pp. 781-786
    • Imaizumi, A.1    Suzuki, Y.2    Ono, S.3    Sato, Y.4    Sato, H.5
  • 24
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: A thrifty, specific pathway for large virulence proteins
    • Jacob-Dubuisson, F., Locht, C. Antoine, R. (2001) Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Mol Microbiol 40 : 306 313.
    • (2001) Mol Microbiol , vol.40 , pp. 306-313
    • Jacob-Dubuisson, F.1    Locht, C.2    Antoine, R.3
  • 26
    • 50149107174 scopus 로고    scopus 로고
    • Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
    • Jiang, J., Zhang, X., Chen, Y., Wu, Y., Zhou, Z.H., Chang, Z. Sui, S.F. (2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc Natl Acad Sci USA 105 : 11939 11944.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11939-11944
    • Jiang, J.1    Zhang, X.2    Chen, Y.3    Wu, Y.4    Zhou, Z.H.5    Chang, Z.6    Sui, S.F.7
  • 27
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker, M., Schuster, C.C., McDonnell, A.V., Sorg, K.A., Finn, M.C., Berger, B. Clark, P.L. (2006) Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc Natl Acad Sci USA 103 : 4918 4923.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4918-4923
    • Junker, M.1    Schuster, C.C.2    McDonnell, A.V.3    Sorg, K.A.4    Finn, M.C.5    Berger, B.6    Clark, P.L.7
  • 28
    • 0034757560 scopus 로고    scopus 로고
    • Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins
    • Kajava, A.V., Cheng, N., Cleaver, R., Kessel, M., Simon, M.N., Willery, E., et al. (2001) Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins. Mol Microbiol 42 : 279 292.
    • (2001) Mol Microbiol , vol.42 , pp. 279-292
    • Kajava, A.V.1    Cheng, N.2    Cleaver, R.3    Kessel, M.4    Simon, M.N.5    Willery, E.6
  • 29
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: The role of the BAM complex in outer membrane protein assembly
    • Knowles, T.J., Scott-Tucker, A., Overduin, M. Henderson, I.R. (2009) Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol 7 : 206 214.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 30
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M.E., Elzer, P.H., Hill, D.S., Robertson, G.T., Farris, M.A., Roop, R.M. Peterson, K.M. (1995) Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166 : 175 176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop, R.M.6    Peterson, K.M.7
  • 31
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M. Clausen, T. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416 : 455 459.
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 32
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer, T., Sawa, J., Schafer, E., Saibil, H.R., Ehrmann, M. Clausen, T. (2008a) Structural basis for the regulated protease and chaperone function of DegP. Nature 453 : 885 890.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 33
    • 45549098563 scopus 로고    scopus 로고
    • Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins
    • Krojer, T., Pangerl, K., Kurt, J., Sawa, J., Stingl, C., Mechtler, K., et al. (2008b) Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins. Proc Natl Acad Sci USA 105 : 7702 7707.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7702-7707
    • Krojer, T.1    Pangerl, K.2    Kurt, J.3    Sawa, J.4    Stingl, C.5    Mechtler, K.6
  • 34
    • 0031798664 scopus 로고    scopus 로고
    • N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin
    • Lambert-Buisine, C., Willery, E., Locht, C. Jacob-Dubuisson, F. (1998) N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin. Mol Microbiol 28 : 1283 1293.
    • (1998) Mol Microbiol , vol.28 , pp. 1283-1293
    • Lambert-Buisine, C.1    Willery, E.2    Locht, C.3    Jacob-Dubuisson, F.4
  • 35
    • 0019473245 scopus 로고
    • Genetic and biochemical characterization of periplasmic-leaky mutants of Escherichia coli K-12
    • Lazzaroni, J.C. Portalier, R.C. (1981) Genetic and biochemical characterization of periplasmic-leaky mutants of Escherichia coli K-12. J Bacteriol 145 : 1351 1358.
    • (1981) J Bacteriol , vol.145 , pp. 1351-1358
    • Lazzaroni, J.C.1    Portalier, R.C.2
  • 36
    • 0023808092 scopus 로고
    • Sequence analysis and regulation of the htrA gene of Escherichia coli: A sigma 32-independent mechanism of heat-inducible transcription
    • Lipinska, B., Sharma, S. Georgopoulos, C. (1988) Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mechanism of heat-inducible transcription. Nucleic Acids Res 16 : 10053 10067.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10053-10067
    • Lipinska, B.1    Sharma, S.2    Georgopoulos, C.3
  • 37
    • 0024519269 scopus 로고
    • Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
    • Lipinska, B., Fayet, O., Baird, L. Georgopoulos, C. (1989) Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J Bacteriol 171 : 1574 1584.
    • (1989) J Bacteriol , vol.171 , pp. 1574-1584
    • Lipinska, B.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 38
    • 0026706341 scopus 로고
    • Common accessory genes for the Bordetella pertussis filamentous hemagglutinin and fimbriae share sequence similarities with the papC and papD gene families
    • Locht, C., Geoffroy, M.-C. Renauld, G. (1992) Common accessory genes for the Bordetella pertussis filamentous hemagglutinin and fimbriae share sequence similarities with the papC and papD gene families. EMBO J 11 : 3175 3183.
    • (1992) EMBO J , vol.11 , pp. 3175-3183
    • Locht, C.1    Geoffroy, M.-C.2    Renauld, G.3
  • 39
    • 33846037385 scopus 로고    scopus 로고
    • Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response
    • McBroom, A.J. Kuehn, M.J. (2007) Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response. Mol Microbiol 63 : 545 558.
    • (2007) Mol Microbiol , vol.63 , pp. 545-558
    • McBroom, A.J.1    Kuehn, M.J.2
  • 40
    • 33749994939 scopus 로고    scopus 로고
    • Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion
    • Mazar, J. Cotter, P.A. (2006) Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion. Mol Microbiol 62 : 641 654.
    • (2006) Mol Microbiol , vol.62 , pp. 641-654
    • Mazar, J.1    Cotter, P.A.2
  • 41
    • 33644871665 scopus 로고    scopus 로고
    • Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore
    • Méli, A.C., Hodak, H., Clantin, B., Locht, C., Molle, G., Jacob-Dubuisson, F. Saint, N. (2006) Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore. J Biol Chem 281 : 158 166.
    • (2006) J Biol Chem , vol.281 , pp. 158-166
    • Méli, A.C.1    Hodak, H.2    Clantin, B.3    Locht, C.4    Molle, G.5    Jacob-Dubuisson, F.6    Saint, N.7
  • 42
    • 0028070016 scopus 로고
    • Surface-associated filamentous hemagglutinin induces autoagglutination of Bordetella pertussis
    • Menozzi, F.D., Boucher, P.E., Riveau, G., Gantiez, C. Locht, C. (1994) Surface-associated filamentous hemagglutinin induces autoagglutination of Bordetella pertussis. Infect Immun 62 : 4261 4269. (Pubitemid 24301951)
    • (1994) Infection and Immunity , vol.62 , Issue.10 , pp. 4261-4269
    • Menozzi, F.D.1    Boucher, P.E.2    Riveau, G.3    Gantiez, C.4    Locht, C.5
  • 43
    • 0033870158 scopus 로고    scopus 로고
    • Overexpression of protease-deficient DegP (S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background
    • Misra, R., CastilloKeller, M. Deng, M. (2000) Overexpression of protease-deficient DegP (S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background. J Bacteriol 182 : 4882 4888.
    • (2000) J Bacteriol , vol.182 , pp. 4882-4888
    • Misra, R.1    Castillokeller, M.2    Deng, M.3
  • 45
    • 0037338681 scopus 로고    scopus 로고
    • A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain
    • Oliver, D.C., Huang, G., Nodel, E., Pleasance, S. Fernandez, R.C. (2003) A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol Microbiol 47 : 1367 1383.
    • (2003) Mol Microbiol , vol.47 , pp. 1367-1383
    • Oliver, D.C.1    Huang, G.2    Nodel, E.3    Pleasance, S.4    Fernandez, R.C.5
  • 46
    • 0346727130 scopus 로고    scopus 로고
    • Evolutionary conservation of biogenesis of beta-barrel membrane proteins
    • Paschen, S.A., Waizenegger, T., Stan, T., Preuss, M., Cyrklaff, M., Hell, K., et al. (2003) Evolutionary conservation of biogenesis of beta-barrel membrane proteins. Nature 426 : 862 866.
    • (2003) Nature , vol.426 , pp. 862-866
    • Paschen, S.A.1    Waizenegger, T.2    Stan, T.3    Preuss, M.4    Cyrklaff, M.5    Hell, K.6
  • 47
    • 33746002324 scopus 로고    scopus 로고
    • The SlyB outer membrane lipoprotein of Burkholderia multivorans contributes to membrane integrity
    • Plesa, M., Hernalsteens, J.P., Vandenbussche, G., Ruysschaert, J.M. Cornelis, P. (2006) The SlyB outer membrane lipoprotein of Burkholderia multivorans contributes to membrane integrity. Res Microbiol 157 : 582 592.
    • (2006) Res Microbiol , vol.157 , pp. 582-592
    • Plesa, M.1    Hernalsteens, J.P.2    Vandenbussche, G.3    Ruysschaert, J.M.4    Cornelis, P.5
  • 48
    • 0036839640 scopus 로고    scopus 로고
    • Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread
    • Purdy, G.E., Hong, M. Payne, S.M. (2002) Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread. Infect Immun 70 : 6355 6364.
    • (2002) Infect Immun , vol.70 , pp. 6355-6364
    • Purdy, G.E.1    Hong, M.2    Payne, S.M.3
  • 49
    • 34547643207 scopus 로고    scopus 로고
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA
    • Purdy, G.E., Fisher, C.R. Payne, S.M. (2007) IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA. J Bacteriol 189 : 5566 5573.
    • (2007) J Bacteriol , vol.189 , pp. 5566-5573
    • Purdy, G.E.1    Fisher, C.R.2    Payne, S.M.3
  • 50
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in Gram-negative bacteria
    • Quandt, J. Hynes, M.F. (1993) Versatile suicide vectors which allow direct selection for gene replacement in Gram-negative bacteria. Gene 127 : 15 21.
    • (1993) Gene , vol.127 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 51
    • 0033106492 scopus 로고    scopus 로고
    • The sigmaE and Cpx regulatory pathways: Overlapping but distinct envelope stress responses
    • Raivio, T.L. Silhavy, T.J. (1999) The sigmaE and Cpx regulatory pathways: overlapping but distinct envelope stress responses. Curr Opin Microbiol 2 : 159 165.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 159-165
    • Raivio, T.L.1    Silhavy, T.J.2
  • 52
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • Sklar, J.G., Wu, T., Kahne, D. Silhavy, T.J. (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev 21 : 2473 2484.
    • (2007) Genes Dev , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 53
    • 34447644224 scopus 로고    scopus 로고
    • Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock
    • Skorko-Glonek, J., Laskowska, E., Sobiecka-Szkatula, A. Lipinska, B. (2007) Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock. Arch Biochem Biophys 464 : 80 89.
    • (2007) Arch Biochem Biophys , vol.464 , pp. 80-89
    • Skorko-Glonek, J.1    Laskowska, E.2    Sobiecka-Szkatula, A.3    Lipinska, B.4
  • 54
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., Beil, A. Ehrmann, M. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97 : 339 347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 55
    • 0031963491 scopus 로고    scopus 로고
    • Secretion of the Haemophilus influenzae HMW1 and HMW2 adhesins involves a periplasmic intermediate and requires the HMWB and HMWC proteins
    • St Geme, J.W., 3rd. Grass, S. (1998) Secretion of the Haemophilus influenzae HMW1 and HMW2 adhesins involves a periplasmic intermediate and requires the HMWB and HMWC proteins. Mol Microbiol 27 : 617 630.
    • (1998) Mol Microbiol , vol.27 , pp. 617-630
    • St Geme III, J.W.1    Grass, S.2
  • 56
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch, K.L., Johnson, K. Beckwith, J. (1989) Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J Bacteriol 171 : 2689 2696.
    • (1989) J Bacteriol , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 57
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton, T.A. Sousa, M.C. (2004) Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol Cell 15 : 367 374.
    • (2004) Mol Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 58
    • 35649021756 scopus 로고    scopus 로고
    • The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion
    • 3rd
    • Yeo, H.J., Yokoyama, T., Walkiewicz, K., Kim, Y., Grass, S. Geme, J.W., 3rd (2007) The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion. J Biol Chem 282 : 31076 31084.
    • (2007) J Biol Chem , vol.282 , pp. 31076-31084
    • Yeo, H.J.1    Yokoyama, T.2    Walkiewicz, K.3    Kim, Y.4    Grass, S.5    Geme, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.