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Volumn 5, Issue , 2014, Pages

Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN; PROTEIN FHAC; PROTEIN TPSA; PROTEIN TPSB; PROTEOLIPOSOME; UNCLASSIFIED DRUG; PROTEOLIPID; PROTEOLIPOSOMES; TYPE V SECRETION SYSTEM;

EID: 84923371062     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6396     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: A semantic awareness issue
    • Desvaux, M., Hebraud, M., Talon, R. & Henderson, I. R. Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol. 17, 139-145 (2009).
    • (2009) Trends Microbiol. , vol.17 , pp. 139-145
    • Desvaux, M.1    Hebraud, M.2    Talon, R.3    Henderson, I.R.4
  • 2
    • 33749186636 scopus 로고    scopus 로고
    • Secretion by numbers: Protein traffic in prokaryotes
    • Economou, A. et al. Secretion by numbers: protein traffic in prokaryotes. Mol. Microbiol. 62, 308-319 (2006).
    • (2006) Mol. Microbiol. , vol.62 , pp. 308-319
    • Economou, A.1
  • 3
    • 84866912780 scopus 로고    scopus 로고
    • Protein traffic in gram-negative bacteria-how exported and secreted proteins find their way
    • Dalbey, R. E. & Kuhn, A. Protein traffic in Gram-negative bacteria-how exported and secreted proteins find their way. FEMS Microbiol. Rev. 36, 1023-1045 (2012).
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 1023-1045
    • Dalbey, R.E.1    Kuhn, A.2
  • 4
    • 84879888089 scopus 로고    scopus 로고
    • Protein translocation across the inner membrane of gramnegative bacteria: The sec and tat dependent protein transport pathways
    • Kudva, R. et al. Protein translocation across the inner membrane of Gramnegative bacteria: the Sec and Tat dependent protein transport pathways. Res. Microbiol. 164, 505-534 (2013).
    • (2013) Res. Microbiol. , vol.164 , pp. 505-534
    • Kudva, R.1
  • 5
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson, I. R. & Nataro, J. P. Virulence functions of autotransporter proteins. Infect. Immun. 69, 1231-1243 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 9
    • 35848952765 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria via the autotransporter pathway
    • Dautin, N. & Bernstein, H. D. Protein secretion in gram-negative bacteria via the autotransporter pathway. Annu. Rev. Microbiol. 61, 89-112 (2007).
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 89-112
    • Dautin, N.1    Bernstein, H.D.2
  • 10
    • 79959468179 scopus 로고    scopus 로고
    • Beta-barrel membrane protein assembly by the bam complex
    • Hagan, C. L., Silhavy, T. J. & Kahne, D. beta-Barrel membrane protein assembly by the Bam complex. Annu. Rev. Biochem. 80, 189-210 (2011).
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 11
    • 84861451226 scopus 로고    scopus 로고
    • The bacterial outer membrane beta-barrel assembly machinery
    • Kim, K. H., Aulakh, S. & Paetzel, M. The bacterial outer membrane beta-barrel assembly machinery. Protein Sci. 21, 751-768 (2012).
    • (2012) Protein Sci. , vol.21 , pp. 751-768
    • Kim, K.H.1    Aulakh, S.2    Paetzel, M.3
  • 12
    • 84869495206 scopus 로고    scopus 로고
    • Evolution of the beta-barrel assembly machinery
    • Webb, C. T., Heinz, E. & Lithgow, T. Evolution of the beta-barrel assembly machinery. Trends Microbiol. 20, 612-620 (2012).
    • (2012) Trends Microbiol. , vol.20 , pp. 612-620
    • Webb, C.T.1    Heinz, E.2    Lithgow, T.3
  • 13
    • 78651374569 scopus 로고    scopus 로고
    • Omp85 in eukaryotic systems: One protein family with distinct functions
    • Schleiff, E., Maier, U. G. & Becker, T. Omp85 in eukaryotic systems: one protein family with distinct functions. Biol. Chem. 392, 21-27 (2011).
    • (2011) Biol. Chem. , vol.392 , pp. 21-27
    • Schleiff, E.1    Maier, U.G.2    Becker, T.3
  • 14
    • 68949207040 scopus 로고    scopus 로고
    • Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: Evolutionary conservation and divergence
    • Walther, D. M., Rapaport, D. & Tommassen, J. Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence. Cell. Mol. Life Sci. 66, 2789-2804 (2009).
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2789-2804
    • Walther, D.M.1    Rapaport, D.2    Tommassen, J.3
  • 15
    • 84857644824 scopus 로고    scopus 로고
    • The bam machine: A molecular cooper
    • Ricci, D. P. & Silhavy, T. J. The Bam machine: a molecular cooper. Biochim. Biophys. Acta 1818, 1067-1084 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1067-1084
    • Ricci, D.P.1    Silhavy, T.J.2
  • 16
    • 34548128883 scopus 로고    scopus 로고
    • Structure of the membrane protein fhac: A member of the omp85-tpsb transporter superfamily
    • Clantin, B. et al. Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily. Science 317, 957-961 (2007).
    • (2007) Science , vol.317 , pp. 957-961
    • Clantin, B.1
  • 17
    • 84884419175 scopus 로고    scopus 로고
    • Structural insight into the biogenesis of beta-barrel membrane proteins
    • Noinaj, N. et al. Structural insight into the biogenesis of beta-barrel membrane proteins. Nature 501, 385-390 (2013).
    • (2013) Nature , vol.501 , pp. 385-390
    • Noinaj, N.1
  • 18
    • 84887430811 scopus 로고    scopus 로고
    • The structural basis of autotransporter translocation by tama
    • Gruss, F. et al. The structural basis of autotransporter translocation by TamA. Nat. Struct. Mol. Biol. 20, 1318-1320 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1318-1320
    • Gruss, F.1
  • 19
    • 84863418948 scopus 로고    scopus 로고
    • Two-partner secretion of gram-negative bacteria: A single beta-barrel protein enables transport across the outer membrane
    • Fan, E., Fiedler, S., Jacob-Dubuisson, F. & Muller, M. Two-partner secretion of gram-negative bacteria: a single beta-barrel protein enables transport across the outer membrane. J. Biol. Chem. 287, 2591-2599 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 2591-2599
    • Fan, E.1    Fiedler, S.2    Jacob-Dubuisson, F.3    Muller, M.4
  • 20
    • 79959563974 scopus 로고    scopus 로고
    • Substrate recognition by the potra domains of tpsb transporter fhac
    • Delattre, A. S. et al. Substrate recognition by the POTRA domains of TpsB transporter FhaC. Mol. Microbiol. 81, 99-112 (2011).
    • (2011) Mol. Microbiol. , vol.81 , pp. 99-112
    • Delattre, A.S.1
  • 21
    • 0026683423 scopus 로고
    • In vitro activation of the serratia marcescens hemolysin through modification and complementation
    • Ondraczek, R., Hobbie, S. & Braun, V. In vitro activation of the Serratia marcescens hemolysin through modification and complementation. J. Bacteriol. 174, 5086-5094 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 5086-5094
    • Ondraczek, R.1    Hobbie, S.2    Braun, V.3
  • 22
    • 0031016583 scopus 로고    scopus 로고
    • Lack of functional complementation between bordetella pertussis filamentous hemagglutinin and proteus mirabilis hpma hemolysin secretion machineries
    • Jacob-Dubuisson, F., Buisine, C., Willery, E., RenauldMongenie, G. & Locht, C. Lack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineries. J. Bacteriol. 179, 775-783 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 775-783
    • Jacob-Dubuisson, F.1    Buisine, C.2    Willery, E.3    Renauldmongenie, G.4    Locht, C.5
  • 23
    • 34447529326 scopus 로고    scopus 로고
    • Requirement for yaet in the outer membrane assembly of autotransporter proteins
    • Jain, S. & Goldberg, M. B. Requirement for YaeT in the outer membrane assembly of autotransporter proteins. J. Bacteriol. 189, 5393-5398 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 5393-5398
    • Jain, S.1    Goldberg, M.B.2
  • 24
    • 71449127822 scopus 로고    scopus 로고
    • The bam (omp85) complex is involved in secretion of the autotransporter haemoglobin protease
    • Sauri, A. et al. The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease. Microbiology 155, 3982-3991 (2009).
    • (2009) Microbiology , vol.155 , pp. 3982-3991
    • Sauri, A.1
  • 25
    • 79961138396 scopus 로고    scopus 로고
    • The essential beta-barrel assembly machinery complex components bamd and bama are required for autotransporter biogenesis
    • Rossiter, A. E. et al. The essential beta-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis. J. Bacteriol. 193, 4250-4253 (2011).
    • (2011) J. Bacteriol. , vol.193 , pp. 4250-4253
    • Rossiter, A.E.1
  • 26
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with bama during its translocation across the bacterial outer membrane
    • Ieva, R. & Bernstein, H. D. Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane. Proc. Natl Acad. Sci. USA 106, 19120-19125 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 27
    • 79961225871 scopus 로고    scopus 로고
    • Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain
    • Ieva, R., Tian, P., Peterson, J. H. & Bernstein, H. D. Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain. Proc. Natl Acad. Sci. USA 108, E383-E391 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. E383-E391
    • Ieva, R.1    Tian, P.2    Peterson, J.H.3    Bernstein, H.4
  • 29
    • 0032940207 scopus 로고    scopus 로고
    • The major phase-variable outer membrane protein of escherichia coli structurally resembles the immunoglobulin a1 protease class of exported protein and is regulated by a novel mechanism involving dam and OXYR
    • Henderson, I. R. & Owen, P. The major phase-variable outer membrane protein of Escherichia coli structurally resembles the immunoglobulin A1 protease class of exported protein and is regulated by a novel mechanism involving Dam and OxyR. J. Bacteriol. 181, 2132-2141 (1999).
    • (1999) J. Bacteriol , vol.181 , pp. 2132-2141
    • Henderson, I.R.1    Owen, P.2
  • 30
    • 3242883431 scopus 로고    scopus 로고
    • Predtmbb: A web server for predicting the topology of beta-barrel outer membrane proteins
    • Bagos, P. G., Liakopoulos, T. D., Spyropoulos, I. C. & Hamodrakas, S. J. PREDTMBB: a web server for predicting the topology of beta-barrel outer membrane proteins. Nucleic Acids Res. 32, W400-W404 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. W400-W404
    • Bagos, P.G.1    Liakopoulos, T.D.2    Spyropoulos, I.C.3    Hamodrakas, S.J.4
  • 31
    • 0017037714 scopus 로고
    • Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from escherichia coli k-12
    • Nakamura, K. & Mizushima, S. Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12. J. Biochem. 80, 1411-1422 (1976).
    • (1976) J. Biochem. , vol.80 , pp. 1411-1422
    • Nakamura, K.1    Mizushima, S.2
  • 32
    • 77956374052 scopus 로고    scopus 로고
    • Assembly of outer-membrane proteins in bacteria and mitochondria
    • Tommassen, J. Assembly of outer-membrane proteins in bacteria and mitochondria. Microbiology 156, 2587-2596 (2010).
    • (2010) Microbiology , vol.156 , pp. 2587-2596
    • Tommassen, J.1
  • 33
    • 0042878499 scopus 로고    scopus 로고
    • Membrane protein folding on the example of outer membrane protein a of escherichia coli
    • Kleinschmidt, J. H. Membrane protein folding on the example of outer membrane protein A of Escherichia coli. Cell. Mol. Life Sci. 60, 1547-1558 (2003).
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1547-1558
    • Kleinschmidt, J.H.1
  • 34
    • 55549120907 scopus 로고    scopus 로고
    • Beta-barrel proteins that reside in the escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
    • Burgess, N. K., Dao, T. P., Stanley, A. M. & Fleming, K. G. beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro. J. Biol. Chem. 283, 26748-26758 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 26748-26758
    • Burgess, N.K.1    Dao, T.P.2    Stanley, A.M.3    Fleming, K.G.4
  • 35
    • 65349145827 scopus 로고    scopus 로고
    • Biogenesis of outer membranes in gram-negative bacteria
    • Tokuda, H. Biogenesis of outer membranes in Gram-negative bacteria. Biosci. Biotechnol. Biochem. 73, 465-473 (2009).
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 465-473
    • Tokuda, H.1
  • 36
    • 84860719904 scopus 로고    scopus 로고
    • Discovery of an archetypal protein transport system in bacterial outer membranes
    • Selkrig, J. et al. Discovery of an archetypal protein transport system in bacterial outer membranes. Nat. Struct. Mol. Biol. 19, 506-510 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 506-510
    • Selkrig, J.1
  • 37
    • 84887430811 scopus 로고    scopus 로고
    • The structural basis of autotransporter translocation by tama
    • Gruss, F. et al. The structural basis of autotransporter translocation by TamA. Nat. Struct. Mol. Biol. 20, 1318-U1247 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1318-U1247
    • Gruss, F.1
  • 38
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M. & Tommassen, J. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299, 262-265 (2003).
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 39
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in escherichia coli
    • Wu, T. et al. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121, 235-245 (2005).
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1
  • 40
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan, C. L., Kim, S. & Kahne, D. Reconstitution of outer membrane protein assembly from purified components. Science 328, 890-892 (2010).
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 41
    • 33644871665 scopus 로고    scopus 로고
    • Channel properties of tpsb transporter fhac point to two functional domains with a c-terminal protein-conducting pore
    • Meli, A. C. et al. 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).
    • (2006) J. Biol. Chem. , vol.281 , pp. 158-166
    • Meli, A.C.1
  • 42
    • 84899620112 scopus 로고    scopus 로고
    • Secretion and activation of the serratia marcescens hemolysin by structurally defined shlb mutants
    • Pramanik, A., Konninger, U., Selvam, A. & Braun, V. Secretion and activation of the Serratia marcescens hemolysin by structurally defined ShlB mutants. Int. J. Med. Microbiol. 304, 351-359 (2013).
    • (2013) Int. J. Med. Microbiol. , vol.304 , pp. 351-359
    • Pramanik, A.1    Konninger, U.2    Selvam, A.3    Braun, V.4
  • 43
    • 0038105593 scopus 로고    scopus 로고
    • Skp a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schafer, U., Beck, K. & Muller, M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274, 24567-24574 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schafer, U.1    Beck, K.2    Muller, M.3
  • 44
    • 0030029213 scopus 로고    scopus 로고
    • Amino-terminal maturation of the bordetella pertussis filamentous haemagglutinin
    • Jacob-Dubuisson, F. et al. Amino-terminal maturation of the Bordetella pertussis filamentous haemagglutinin. Mol. Microbiol. 19, 65-78 (1996).
    • (1996) Mol. Microbiol. , vol.19 , pp. 65-78
    • Jacob-Dubuisson, F.1
  • 45
    • 36549072024 scopus 로고    scopus 로고
    • In vitro analysis of the bacterial twin-Arginine-dependent protein export
    • Moser, M., Panahandeh, S., Holzapfel, E. & Muller, M. In vitro analysis of the bacterial twin-Arginine-dependent protein export. Methods Mol. Biol. 390, 63-79 (2007).
    • (2007) Methods Mol. Biol. , vol.390 , pp. 63-79
    • Moser, M.1    Panahandeh, S.2    Holzapfel, E.3    Muller, M.4
  • 46
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor omp85 recognizes its outer membrane protein substrates by a species-specific c-terminal motif
    • Robert, V. et al. Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif. PLoS Biol. 4, e377 (2006).
    • (2006) PLoS Biol. , vol.4 , pp. e377
    • Robert, V.1


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