메뉴 건너뛰기




Volumn 290, Issue 16, 2015, Pages 10104-10116

Multiple driving forces required for efficient secretion of autotransporter virulence proteins

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; C (PROGRAMMING LANGUAGE); PHYSIOLOGY; PROTEINS;

EID: 84927721216     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.629170     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 84857148914 scopus 로고    scopus 로고
    • From self sufficiency to dependence: Mechanisms and factors important for autotransporter biogenesis
    • Leyton, D. L., Rossiter, A. E., and Henderson, I. R. (2012) From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis. Nat. Rev. Microbiol. 10, 213-225
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 213-225
    • Leyton, D.L.1    Rossiter, A.E.2    Henderson, I.R.3
  • 2
    • 35848952765 scopus 로고    scopus 로고
    • Protein secretion in Gram-negative bacteria via the autotransporter pathway
    • Dautin, N., and Bernstein, H. D. (2007) Protein secretion in Gram-negative bacteria via the autotransporter pathway. Annu. Rev. Microbiol. 61, 89-112
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 89-112
    • Dautin, N.1    Bernstein, H.D.2
  • 3
    • 77957354322 scopus 로고    scopus 로고
    • Extracellular production of recombinant proteins using bacterial autotransporters
    • Jong, W. S., Saurí, A., and Luirink, J. (2010) Extracellular production of recombinant proteins using bacterial autotransporters. Curr. Opin. Biotechnol. 21, 646-652
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 646-652
    • Jong, W.S.1    Saurí, A.2    Luirink, J.3
  • 4
    • 37349047429 scopus 로고    scopus 로고
    • The autodisplay story, from discovery to biotechnical and biomedical applications
    • Jose, J., and Meyer, T. F. (2007) The autodisplay story, from discovery to biotechnical and biomedical applications. Microbiol. Mol. Biol. Rev. 71, 600-619
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 600-619
    • Jose, J.1    Meyer, T.F.2
  • 5
    • 18844384961 scopus 로고    scopus 로고
    • Protein secretion in the absence of ATP: The autotransporter, two-partner secretion and chaperone/usher pathways of Gram-negative bacteria
    • (review)
    • Thanassi, D. G., Stathopoulos, C., Karkal, A., and Li, H. (2005) Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of Gram-negative bacteria (review). Mol. Membr. Biol. 22, 63-72
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 63-72
    • Thanassi, D.G.1    Stathopoulos, C.2    Karkal, A.3    Li, H.4
  • 7
    • 0026511122 scopus 로고
    • Selective extracellular release of cholera toxin B subunit by Escherichia coli: Dissection of Neisseria IgA-mediated outer membrane transport
    • Klauser, T., Pohlner, J., and Meyer, T. F. (1992) Selective extracellular release of cholera toxin B subunit by Escherichia coli: dissection of Neisseria IgA-mediated outer membrane transport. EMBO J. 11, 2327-2335
    • (1992) EMBO J. , vol.11 , pp. 2327-2335
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 8
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin β-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., and Clark, P. L. (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    Schuster, C.C.2    McDonnell, A.V.3    Sorg, K.A.4    Finn, M.C.5    Berger, B.6    Clark, P.L.7
  • 9
    • 78049313288 scopus 로고    scopus 로고
    • Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment
    • Peterson, J. H., Tian, P., Ieva, R., Dautin, N., and Bernstein, H. D. (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
  • 10
    • 84857175966 scopus 로고    scopus 로고
    • ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein
    • Renn, J. P., Junker, M., Besingi, R. N., Braselmann, E., and Clark, P. L. (2012) ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein. Chem. Biol. 19, 287-296
    • (2012) Chem. Biol. , vol.19 , pp. 287-296
    • Renn, J.P.1    Junker, M.2    Besingi, R.N.3    Braselmann, E.4    Clark, P.L.5
  • 11
    • 84860134831 scopus 로고    scopus 로고
    • Autotransporters: The cellular environment reshapes a folding mechanism to promote protein transport
    • Braselmann, E., and Clark, P. L. (2012) Autotransporters: the cellular environment reshapes a folding mechanism to promote protein transport. J. Phys. Chem. Lett. 3, 1063-1071
    • (2012) J. Phys. Chem. Lett. , vol.3 , pp. 1063-1071
    • Braselmann, E.1    Clark, P.L.2
  • 12
    • 60649098853 scopus 로고    scopus 로고
    • Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion
    • Junker, M., Besingi, R. N., and Clark, P. L. (2009) Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion. Mol. Microbiol. 71, 1323-1332
    • (2009) Mol. Microbiol. , vol.71 , pp. 1323-1332
    • Junker, M.1    Besingi, R.N.2    Clark, P.L.3
  • 15
    • 84902327125 scopus 로고    scopus 로고
    • Assembly of β-barrel proteins into bacterial outer membranes
    • Selkrig, J., Leyton, D. L., Webb, C. T., and Lithgow, T. (2014) Assembly of β-barrel proteins into bacterial outer membranes. Biochim. Biophys. Acta 1843, 1542-1550
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1542-1550
    • Selkrig, J.1    Leyton, D.L.2    Webb, C.T.3    Lithgow, T.4
  • 16
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • Ruiz-Perez, F., Henderson, I. R., Leyton, D. L., Rossiter, A. E., Zhang, Y., and Nataro, J. P. (2009) Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. J. Bacteriol. 191, 6571-6583
    • (2009) J. Bacteriol. , vol.191 , pp. 6571-6583
    • Ruiz-Perez, F.1    Henderson, I.R.2    Leyton, D.L.3    Rossiter, A.E.4    Zhang, Y.5    Nataro, J.P.6
  • 17
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane
    • Ieva, R., and Bernstein, H. D. (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
  • 19
    • 84919397096 scopus 로고    scopus 로고
    • Reconstitution of bacterial autotransporter assembly using purified components
    • Roman-Hernandez, G., Peterson, J. H., and Bernstein, H. D. (2014) Reconstitution of bacterial autotransporter assembly using purified components. eLife 3, e04234
    • (2014) eLife , vol.3 , pp. e04234
    • Roman-Hernandez, G.1    Peterson, J.H.2    Bernstein, H.D.3
  • 21
    • 84856726498 scopus 로고    scopus 로고
    • Estimating the size of the active translocation pore of an autotransporter
    • Saurí, A., Ten Hagen-Jongman, C. M., van Ulsen, P., and Luirink, J. (2012) Estimating the size of the active translocation pore of an autotransporter. J. Mol. Biol. 416, 335-345
    • (2012) J. Mol. Biol. , vol.416 , pp. 335-345
    • Saurí, A.1    Ten Hagen-Jongman, C.M.2    Van Ulsen, P.3    Luirink, J.4
  • 23
    • 34247238897 scopus 로고    scopus 로고
    • Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism
    • Dautin, N., Barnard, T. J., Anderson, D. E., and Bernstein, H. D. (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
  • 24
    • 84887306808 scopus 로고    scopus 로고
    • Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway
    • Kang'ethe, W., and Bernstein, H. D. (2013) Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway. Proc. Natl. Acad. Sci. U.S.A. 110, E4246-E4255
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. E4246-E4255
    • Kang'Ethe, W.1    Bernstein, H.D.2
  • 25
    • 84888316691 scopus 로고    scopus 로고
    • An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core
    • Besingi, R. N., Chaney, J. L., and Clark, P. L. (2013) An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core. Mol. Microbiol. 90, 1028-1045
    • (2013) Mol. Microbiol. , vol.90 , pp. 1028-1045
    • Besingi, R.N.1    Chaney, J.L.2    Clark, P.L.3
  • 26
    • 64649088018 scopus 로고    scopus 로고
    • Outer membrane permeability and antibiotic resistance
    • Delcour, A. H. (2009) Outer membrane permeability and antibiotic resistance. Biochim. Biophys. Acta 1794, 808-816
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 808-816
    • Delcour, A.H.1
  • 28
    • 0025244120 scopus 로고
    • Protective surface antigen P69 of Bordetella pertussis: Its characterization and very high level expression in Escherichia coli
    • Makoff, A. J., Oxer, M. D., Ballantine, S. P., Fairweather, N. F., and Charles, I. G. (1990) Protective surface antigen P69 of Bordetella pertussis: its characterization and very high level expression in Escherichia coli. Biotechnology 8, 1030-1033
    • (1990) Biotechnology , vol.8 , pp. 1030-1033
    • Makoff, A.J.1    Oxer, M.D.2    Ballantine, S.P.3    Fairweather, N.F.4    Charles, I.G.5
  • 29
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley, P., Charles, I. G., Fairweather, N. F., and 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
  • 30
    • 77949329716 scopus 로고    scopus 로고
    • Slow formation of aggregation-resistant β-sheet folding intermediates
    • Junker, M., and Clark, P. L. (2010) Slow formation of aggregation-resistant β-sheet folding intermediates. Proteins 78, 812-824
    • (2010) Proteins , vol.78 , pp. 812-824
    • Junker, M.1    Clark, P.L.2
  • 31
    • 33645429016 scopus 로고
    • Exact stochastic simulation of coupled chemical reactions
    • Gillespie, D. T. (1977) Exact stochastic simulation of coupled chemical reactions. J. Phys. Chem. 81, 2340-2361
    • (1977) J. Phys. Chem. , vol.81 , pp. 2340-2361
    • Gillespie, D.T.1
  • 32
    • 38949164415 scopus 로고    scopus 로고
    • Algorithms and software for stochastic simulation of biochemical reacting systems
    • Li, H., Cao, Y., Petzold, L. R., and Gillespie, D. T. (2008) Algorithms and software for stochastic simulation of biochemical reacting systems. Biotechnol. Prog. 24, 56-61
    • (2008) Biotechnol. Prog. , vol.24 , pp. 56-61
    • Li, H.1    Cao, Y.2    Petzold, L.R.3    Gillespie, D.T.4
  • 33
    • 47749087527 scopus 로고    scopus 로고
    • A conserved stable core structure in the passenger domain β-helix of autotransporter virulence proteins
    • Renn, J. P., and Clark, P. L. (2008) A conserved stable core structure in the passenger domain β-helix of autotransporter virulence proteins. Biopolymers 89, 420-427
    • (2008) Biopolymers , vol.89 , pp. 420-427
    • Renn, J.P.1    Clark, P.L.2
  • 34
    • 79551689315 scopus 로고    scopus 로고
    • A rapid protein folding assay for the bacterial periplasm
    • Mansell, T. J., Linderman, S. W., Fisher, A. C., and DeLisa, M. P. (2010) A rapid protein folding assay for the bacterial periplasm. Protein Sci. 19, 1079-1090
    • (2010) Protein Sci. , vol.19 , pp. 1079-1090
    • Mansell, T.J.1    Linderman, S.W.2    Fisher, A.C.3    DeLisa, M.P.4
  • 35
    • 3042784273 scopus 로고    scopus 로고
    • Creating random mutagenesis libraries by megaprimer PCR of whole plasmid (MEGAWHOP)
    • Miyazaki, K. (2003) Creating random mutagenesis libraries by megaprimer PCR of whole plasmid (MEGAWHOP). Methods Mol. Biol. 231, 23-28
    • (2003) Methods Mol. Biol. , vol.231 , pp. 23-28
    • Miyazaki, K.1
  • 36
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigenantibody complexes by enzyme-linked immunosorbent assay
    • Friguet, B., Chaffotte, A. F., Djavadi-Ohaniance, L., and Goldberg, M. E. (1985) Measurements of the true affinity constant in solution of antigenantibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods 77, 305-319
    • (1985) J. Immunol. Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 37
    • 0017109844 scopus 로고
    • Outer membrane of Gram-negative bacteria. XII. Molecular-sieving function of cell wall
    • Decad, G. M., and Nikaido, H. (1976) Outer membrane of Gram-negative bacteria. XII. Molecular-sieving function of cell wall. J. Bacteriol. 128, 325-336
    • (1976) J. Bacteriol. , vol.128 , pp. 325-336
    • Decad, G.M.1    Nikaido, H.2
  • 39
    • 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., and 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
  • 40
    • 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 Nataro, J. P. (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
  • 41
    • 84890278171 scopus 로고    scopus 로고
    • Stepwise folding of an autotransporter passenger domain is not essential for its secretion
    • Kang'ethe, W., and Bernstein, H. D. (2013) Stepwise folding of an autotransporter passenger domain is not essential for its secretion. J. Biol. Chem. 288, 35028-35038
    • (2013) J. Biol. Chem. , vol.288 , pp. 35028-35038
    • Kang'Ethe, W.1    Bernstein, H.D.2
  • 42
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease β-domain: Conformation-dependent outer membrane translocation
    • Klauser, T., Pohlner, J., and Meyer, T. F. (1990) Extracellular transport of cholera toxin B subunit using Neisseria IgA protease β-domain: conformation-dependent outer membrane translocation. EMBOJ. 9, 1991-1999
    • (1990) EMBOJ , vol.9 , pp. 1991-1999
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 43
    • 0029621229 scopus 로고
    • Extracellular transport of VirG protein in Shigella
    • Suzuki, T., Lett, M.-C., and Sasakawa, C. (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
  • 44
    • 33845452751 scopus 로고    scopus 로고
    • Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I)
    • Charbonneau, M.-E., Berthiaume, F., and Mourez, M. (2006) Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I). J. Bacteriol. 188, 8504-8512
    • (2006) J. Bacteriol. , vol.188 , pp. 8504-8512
    • Charbonneau, M.-E.1    Berthiaume, F.2    Mourez, M.3
  • 45
    • 84872538583 scopus 로고    scopus 로고
    • Energetic cost of protein import across the envelope membranes of chloroplasts
    • Shi, L.-X., and Theg, S. M. (2013) Energetic cost of protein import across the envelope membranes of chloroplasts. Proc. Natl. Acad. Sci. U.S.A. 110, 930-935
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 930-935
    • Shi, L.-X.1    Theg, S.M.2
  • 48
    • 84875037470 scopus 로고    scopus 로고
    • Membrane protein thermodynamic stability
    • may serve as the energy sink for sorting in the periplasm.
    • Moon, C. P., Zaccai, N. R., Fleming, P. J., Gessmann, D., and Fleming, K. G. (2013) Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm. Proc. Natl. Acad. Sci. U.S.A. 110, 4285-4290
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 4285-4290
    • Moon, C.P.1    Zaccai, N.R.2    Fleming, P.J.3    Gessmann, D.4    Fleming, K.G.5
  • 52
    • 46049118792 scopus 로고    scopus 로고
    • Mutagenesis of the Shigella flexneri autotransporter IcsA reveals novel functional regions involved in IcsA biogenesis and recruitment of host neural Wiscott-Aldrich syndrome protein
    • May, K. L., and Morona, R. (2008) Mutagenesis of the Shigella flexneri autotransporter IcsA reveals novel functional regions involved in IcsA biogenesis and recruitment of host neural Wiscott-Aldrich syndrome protein. J. Bacteriol. 190, 4666-4676
    • (2008) J. Bacteriol. , vol.190 , pp. 4666-4676
    • May, K.L.1    Morona, R.2
  • 53
    • 79954490781 scopus 로고    scopus 로고
    • Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore
    • Zhai, Y., Zhang, K., Huo, Y., Zhu, Y., Zhou, Q., Lu, J., Black, I., Pang, X., Roszak, A. W., Zhang, X., Isaacs, N. W., and Sun, F. (2011) Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore. Biochem. J. 435, 577-587
    • (2011) Biochem. J. , vol.435 , pp. 577-587
    • Zhai, Y.1    Zhang, K.2    Huo, Y.3    Zhu, Y.4    Zhou, Q.5    Lu, J.6    Black, I.7    Pang, X.8    Roszak, A.W.9    Zhang, X.10    Isaacs, N.W.11    Sun, F.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.