메뉴 건너뛰기




Volumn 193, Issue 15, 2011, Pages 3748-3756

Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain

Author keywords

[No Author keywords available]

Indexed keywords

PERTACTIN; SERINE PROTEINASE;

EID: 79960436639     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05070-11     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0025357506 scopus 로고
    • SecY protein, a membrane-embedded secretion factor of E. coli, is cleaved by the OmpT protease in vitro
    • Akiyama, Y., and K. Ito. 1990. SecY protein, a membrane-embedded secretion factor of E. coli, is cleaved by the OmpT protease in vitro. Biochem. Biophys. Res. Commun. 167:711-715.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 711-715
    • Akiyama, Y.1    Ito, K.2
  • 2
    • 0030088086 scopus 로고    scopus 로고
    • Site-specific mutagenesis by using an accurate recombinant PCR method
    • Ansaldi, M., M. Lepelletier, and V. Mejean. 1996. Site-specific mutagenesis by using an accurate recombinant PCR method. Anal. Biochem. 234:110-111.
    • (1996) Anal. Biochem. , vol.234 , pp. 110-111
    • Ansaldi, M.1    Lepelletier, M.2    Mejean, V.3
  • 3
    • 36849016945 scopus 로고    scopus 로고
    • Autotransporter structure reveals intra-barrel cleavage followed by conformational changes
    • Barnard, T. J., N. Dautin, P. Lukacik, H. D. Bernstein, and S. K. Buchanan. 2007. Autotransporter structure reveals intra-barrel cleavage followed by conformational changes. Nat. Struct. Mol. Biol. 14:1214-1220.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1214-1220
    • Barnard, T.J.1    Dautin, N.2    Lukacik, P.3    Bernstein, H.D.4    Buchanan, S.K.5
  • 4
    • 84959171477 scopus 로고    scopus 로고
    • posting date. Type V secretion: the autotransporter and two-partner secretion pathways
    • 16 September A. Böck et al. (ed.), ASM Press, Washington, DC. doi:10.1128/ecosal.4.3.6
    • Bernstein, H. D. 16 September 2010, posting date. Type V secretion: the autotransporter and two-partner secretion pathways. In A. Böck et al. (ed.), EcoSal-Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. doi:10.1128/ecosal.4.3.6.
    • (2010) EcoSal-Escherichia coli and Salmonella: cellular and molecular biology
    • Bernstein, H.D.1
  • 5
    • 74349124486 scopus 로고    scopus 로고
    • Sequential translocation of an Escherichia coli two-partner secretion pathway exoprotein across the inner and outer membranes
    • Choi, P. S., and H. D. Bernstein. 2010. Sequential translocation of an Escherichia coli two-partner secretion pathway exoprotein across the inner and outer membranes. Mol. Microbiol. 75:440-451.
    • (2010) Mol. Microbiol. , vol.75 , pp. 440-451
    • Choi, P.S.1    Bernstein, H.D.2
  • 6
    • 34247238897 scopus 로고    scopus 로고
    • Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism
    • Dautin, N., T. J. Barnard, D. E. Anderson, and H. D. Bernstein. 2007. Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism. EMBO J. 26:1942-1952.
    • (2007) EMBO J , vol.26 , pp. 1942-1952
    • Dautin, N.1    Barnard, T.J.2    Anderson, D.E.3    Bernstein, H.D.4
  • 7
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley, P., I. G. Charles, N. F. Fairweather, and N. W. Isaacs. 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
  • 8
    • 36048946721 scopus 로고    scopus 로고
    • Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain
    • Gangwer, K. A., et al. 2007. Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain. Proc. Natl. Acad. Sci. U. S. A. 104:16293-16298.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 16293-16298
    • Gangwer, K.A.1
  • 10
    • 0030693901 scopus 로고    scopus 로고
    • Structural determinants of processing and secretion of the Haemophilus influenzae Hap protein
    • Hendrixson, D. R., M. L. de la Morena, C. Stathopoulos, and J. W. St. Geme III. 1997. Structural determinants of processing and secretion of the Haemophilus influenzae Hap protein. Mol. Microbiol. 26:505-518.
    • (1997) Mol. Microbiol. , vol.26 , pp. 505-518
    • Hendrixson, D.R.1    de la Morena, M.L.2    Stathopoulos, C.3    St. Geme III, J.W.4
  • 11
  • 12
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane
    • Ieva, R., and H. D. Bernstein. 2009. Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane. Proc. Natl. Acad. Sci. U. S. A. 106:19120-19125.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 13
    • 36849048754 scopus 로고    scopus 로고
    • Incorporation of a polypeptide segment into the β-domain pore during the assembly of a bacterial autotransporter
    • Ieva, R., K. M. Skillman, and H. D. Bernstein. 2008. Incorporation of a polypeptide segment into the β-domain pore during the assembly of a bacterial autotransporter. Mol. Microbiol. 67:188-201.
    • (2008) Mol. Microbiol. , vol.67 , pp. 188-201
    • Ieva, R.1    Skillman, K.M.2    Bernstein, H.D.3
  • 14
    • 65649092581 scopus 로고    scopus 로고
    • Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease: the structure of Haemophilus influenzae immunoglobulin A1 protease
    • Johnson, T. A., J. Qiu, A. G. Plaut, and T. Holyoak. 2009. Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease: the structure of Haemophilus influenzae immunoglobulin A1 protease. J. Mol. Biol. 389:559-574.
    • (2009) J. Mol. Biol. , vol.389 , pp. 559-574
    • Johnson, T.A.1    Qiu, J.2    Plaut, A.G.3    Holyoak, T.4
  • 15
    • 33847000902 scopus 로고    scopus 로고
    • Limited tolerance towards folded elements during secretion of the autotransporter Hbp
    • Jong, W. S., et al. 2007. Limited tolerance towards folded elements during secretion of the autotransporter Hbp. Mol. Microbiol. 63:1524-1536.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1524-1536
    • Jong, W.S.1
  • 16
    • 60649098853 scopus 로고    scopus 로고
    • Vectorial transport and folding of an autotransporter virulence protein during outer membrane assembly
    • Junker, M., R. N. Besingi, and P. L. Clark. 2009. Vectorial transport and folding of an autotransporter virulence protein during outer membrane assembly. Mol. Microbiol. 71:1323-1332.
    • (2009) Mol. Microbiol. , vol.71 , pp. 1323-1332
    • Junker, M.1    Besingi, R.N.2    Clark, P.L.3
  • 17
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin β-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker, M., et al. 2006. Pertactin β-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc. Natl. Acad. Sci. U. S. A. 103:4918-4923.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4918-4923
    • Junker, M.1
  • 18
    • 0027136213 scopus 로고
    • Characterization of the Neisseria Iga β-core. The essential unit for outer membrane targeting and extracellular protein secretion
    • Klauser, T., J. Krämer, K. Otzelberger, J. Pohlner, and T. F. Meyer. 1993. Characterization of the Neisseria Iga β-core. The essential unit for outer membrane targeting and extracellular protein secretion. J. Mol. Biol. 234: 579-593.
    • (1993) J. Mol. Biol. , vol.234 , pp. 579-593
    • Klauser, T.1    Krämer, J.2    Otzelberger, K.3    Pohlner, J.4    Meyer, T.F.5
  • 19
    • 33748068126 scopus 로고    scopus 로고
    • Role of the β-helical linker of the C-terminal translocator in the biogenesis of the serine protease subfamily of autotransporters
    • Kostakioti, M., and C. Stathopoulos. 2006. Role of the β-helical linker of the C-terminal translocator in the biogenesis of the serine protease subfamily of autotransporters. Infect. Immun. 74:4961-4969.
    • (2006) Infect. Immun. , vol.74 , pp. 4961-4969
    • Kostakioti, M.1    Stathopoulos, C.2
  • 20
    • 78049375319 scopus 로고    scopus 로고
    • Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters
    • Marín, E., G. Bodelón, and L. Á. Fernández. 2010. Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters. J. Bacteriol. 192:5588-5602.
    • (2010) J. Bacteriol. , vol.192 , pp. 5588-5602
    • Marín, E.1    Bodelón, G.2    Fernández, L.Á.3
  • 21
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng, G., N. K. Surana, J. W. St. Geme III, and G. Waksman. 2006. Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J. 25:2297-2304.
    • (2006) EMBO J , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    St. Geme III, J.W.3    Waksman, G.4
  • 22
    • 21544468024 scopus 로고    scopus 로고
    • Arrangement of the translocator of the autotransporter adhesin involved in diffuse adherence on the bacterial surface
    • Müller, D., et al. 2005. Arrangement of the translocator of the autotransporter adhesin involved in diffuse adherence on the bacterial surface. Infect. Immun. 73:3851-3859.
    • (2005) Infect. Immun. , vol.73 , pp. 3851-3859
    • Müller, D.1
  • 23
    • 0035145396 scopus 로고    scopus 로고
    • Plasmid-encoded toxin of enteroaggregative Escherichia coli is internalized by epithelial cells
    • Navarro-García, F., A. Canizalez-Roman, J. Luna, C. Sears, and J. P. Nataro. 2001. Plasmid-encoded toxin of enteroaggregative Escherichia coli is internalized by epithelial cells. Infect. Immun. 69:1053-1060.
    • (2001) Infect. Immun. , vol.69 , pp. 1053-1060
    • Navarro-García, F.1    Canizalez-Roman, A.2    Luna, J.3    Sears, C.4    Nataro, J.P.5
  • 24
    • 0037224652 scopus 로고    scopus 로고
    • Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter
    • Oliver, D. C., G. Huang, and R. C. Fernandez. 2003. Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter. J. Bacteriol. 185:489-495.
    • (2003) J. Bacteriol. , vol.185 , pp. 489-495
    • Oliver, D.C.1    Huang, G.2    Fernandez, R.C.3
  • 25
    • 1942471665 scopus 로고    scopus 로고
    • Structure of the translocator domain of a bacterial autotransporter
    • Oomen, C. J., et al. 2004. Structure of the translocator domain of a bacterial autotransporter. EMBO J. 23:1257-1266.
    • (2004) EMBO J , vol.23 , pp. 1257-1266
    • Oomen, C.J.1
  • 26
    • 20444435483 scopus 로고    scopus 로고
    • Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli
    • Otto, B. R., et al. 2005. Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. J. Biol. Chem. 280:17339-17345.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17339-17345
    • Otto, B.R.1
  • 27
    • 1342281315 scopus 로고    scopus 로고
    • Identification and molecular characterization of EatA, an autotransporter protein of enterotoxigenic Escherichia coli
    • Patel, S. K., J. Dotson, K. P. Allen, and J. M. Fleckenstein. 2004. Identification and molecular characterization of EatA, an autotransporter protein of enterotoxigenic Escherichia coli. Infect. Immun. 72:1786-1794.
    • (2004) Infect. Immun. , vol.72 , pp. 1786-1794
    • Patel, S.K.1    Dotson, J.2    Allen, K.P.3    Fleckenstein, J.M.4
  • 28
    • 78049313288 scopus 로고    scopus 로고
    • Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment
    • Peterson, J. H., P. Tian, R. Ieva, N. Dautin, and H. D. Bernstein. 2010. Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment. Proc. Natl. Acad. Sci. U. S. A. 107:17739-17744.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 17739-17744
    • Peterson, J.H.1    Tian, P.2    Ieva, R.3    Dautin, N.4    Bernstein, H.D.5
  • 29
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner, J., R. Halter, K. Beyreuther, and T. F. Meyer. 1987. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 325:458-462.
    • (1987) Nature , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 30
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli
    • Sääf, A., M. Monné, J. W. de Gier, and G. von Heijne. 1998. Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli. J. Biol. Chem. 273:30415-30418.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30415-30418
    • Sääf, A.1    Monné, M.2    de Gier, J.W.3    von Heijne, G.4
  • 31
    • 27944445725 scopus 로고    scopus 로고
    • Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter
    • Skillman, K. M., T. J. Barnard, J. H. Peterson, R. Ghirlando, and H. D. Bernstein. 2005. Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter. Mol. Microbiol. 58:945-958.
    • (2005) Mol. Microbiol. , vol.58 , pp. 945-958
    • Skillman, K.M.1    Barnard, T.J.2    Peterson, J.H.3    Ghirlando, R.4    Bernstein, H.D.5
  • 32
    • 0029961503 scopus 로고    scopus 로고
    • Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins
    • Stein, M., B. Kenny, M. A. Stein, and B. B. Finlay. 1996. Characterization of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins. J. Bacteriol. 178:6546-6554.
    • (1996) J. Bacteriol. , vol.178 , pp. 6546-6554
    • Stein, M.1    Kenny, B.2    Stein, M.A.3    Finlay, B.B.4
  • 33
    • 0029621229 scopus 로고
    • Extracellular transport of VirG protein in Shigella
    • Suzuki, T., M. C. Lett, and C. Sasakawa. 1995. Extracellular transport of VirG protein in Shigella. J. Biol. Chem. 270:30874-30880.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30874-30880
    • Suzuki, T.1    Lett, M.C.2    Sasakawa, C.3
  • 34
    • 11844280919 scopus 로고    scopus 로고
    • An unusual signal peptide facilitates the late steps in the biogenesis of a bacterial autotransporter
    • Szabady, R. L., J. H. Peterson, K. M. Skillman, and H. D. Bernstein. 2005. An unusual signal peptide facilitates the late steps in the biogenesis of a bacterial autotransporter. Proc. Natl. Acad. Sci. U. S. A. 102:221-226.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 221-226
    • Szabady, R.L.1    Peterson, J.H.2    Skillman, K.M.3    Bernstein, H.D.4
  • 35
    • 77956916073 scopus 로고    scopus 로고
    • A novel intein-like autoproteolytic mechanism in autotransporter proteins
    • Tajima, N., F. Kawai, S.-Y. Park, and J. R. Tame. 2010. A novel intein-like autoproteolytic mechanism in autotransporter proteins. J. Mol. Biol. 402: 645-656.
    • (2010) J. Mol. Biol. , vol.402 , pp. 645-656
    • Tajima, N.1    Kawai, F.2    Park, S.-Y.3    Tame, J.R.4
  • 36
    • 0031472242 scopus 로고    scopus 로고
    • The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt, N. D., J. A. Newitt, and H. D. Bernstein. 1997. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88:187-196.
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 37
    • 77949323924 scopus 로고    scopus 로고
    • Crystal structure of a full-length autotransporter
    • van den Berg, B. 2010. Crystal structure of a full-length autotransporter. J. Mol. Biol. 396:627-633.
    • (2010) J. Mol. Biol. , vol.396 , pp. 627-633
    • van den Berg, B.1
  • 38
    • 3843078622 scopus 로고    scopus 로고
    • Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger
    • Velarde, J. J., and J. P. Nataro. 2004. Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger. J. Biol. Chem. 279:31495-31504.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31495-31504
    • Velarde, J.J.1    Nataro, J.P.2
  • 39
    • 0037428132 scopus 로고    scopus 로고
    • Role of highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., M. P. Bos, J. Geurtsen, M. Mols, and J. Tommassen. 2003. Role of highly conserved bacterial protein in outer membrane protein assembly. Science 299:262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 40
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T., et al. 2005. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121:235-245.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.