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Volumn 70, Issue 2, 2013, Pages 168-189

Thioredoxin-like proteins in F and other plasmid systems

Author keywords

Disulfide; Isomerase; Oxidase; Plasmid; Reductase; Thioredoxin

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; CCMG PROTEIN; COM1 PROTEIN; CYSTEINE; DISULFIDE; DSBA PROTEIN; DSBB PROTEIN; DSBC PROTEIN; DSBD PROTEIN; DSBG PROTEIN; ISOMERASE; PLASMID DNA; SINGLE STRANDED DNA; STRUCTURAL PROTEIN; THIOL; THIOREDOXIN LIKE PROTEIN; TLPA PROTEIN; TRBB PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR; UNCLASSIFIED DRUG;

EID: 84881025514     PISSN: 0147619X     EISSN: 10959890     Source Type: Journal    
DOI: 10.1016/j.plasmid.2013.05.004     Document Type: Review
Times cited : (14)

References (133)
  • 1
    • 0016748528 scopus 로고
    • Mating aggregates in Escherichia coli conjugation
    • Achtman M. Mating aggregates in Escherichia coli conjugation. J. Bacteriol. 1975, 123:505-515.
    • (1975) J. Bacteriol. , vol.123 , pp. 505-515
    • Achtman, M.1
  • 2
    • 0017751759 scopus 로고
    • Cell-cell interactions in conjugating Escherichia coli: role of traT protein in surface exclusion
    • Achtman M., Kennedy N., et al. Cell-cell interactions in conjugating Escherichia coli: role of traT protein in surface exclusion. Proc. Natl. Acad. Sci. USA 1977, 74:5104-5108.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5104-5108
    • Achtman, M.1    Kennedy, N.2
  • 3
    • 0032989880 scopus 로고    scopus 로고
    • The virulence plasmid of Salmonella typhimurium is self-transmissible
    • Ahmer B.M., Tran M., et al. The virulence plasmid of Salmonella typhimurium is self-transmissible. J. Bacteriol. 1999, 181:1364-1368.
    • (1999) J. Bacteriol. , vol.181 , pp. 1364-1368
    • Ahmer, B.M.1    Tran, M.2
  • 4
    • 0030830073 scopus 로고    scopus 로고
    • A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins
    • Andersen C.L., Matthey-Dupraz A., et al. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol. Microbiol. 1997, 26:121-132.
    • (1997) Mol. Microbiol. , vol.26 , pp. 121-132
    • Andersen, C.L.1    Matthey-Dupraz, A.2
  • 5
    • 77949398282 scopus 로고    scopus 로고
    • F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation
    • Arutyunov D., Arenson B., et al. F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation. J. Bacteriol. 2010, 192:1730-1734.
    • (2010) J. Bacteriol. , vol.192 , pp. 1730-1734
    • Arutyunov, D.1    Arenson, B.2
  • 6
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • Babu M.M., Priya M.L., et al. A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins. J. Bacteriol. 2006, 188:2761-2773.
    • (2006) J. Bacteriol. , vol.188 , pp. 2761-2773
    • Babu, M.M.1    Priya, M.L.2
  • 7
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader M., Muse W., et al. Oxidative protein folding is driven by the electron transport system. Cell 1999, 98:217-227.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2
  • 8
    • 0035794534 scopus 로고    scopus 로고
    • Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA
    • Bader M.W., Hiniker A., et al. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. EMBO J. 2001, 20:1555-1562.
    • (2001) EMBO J. , vol.20 , pp. 1555-1562
    • Bader, M.W.1    Hiniker, A.2
  • 9
    • 16644390231 scopus 로고    scopus 로고
    • Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli
    • Banaszak K., Mechin I., et al. Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli. Acta. Crystallogr. D Biol. Crystallogr. 2004, 60:1747-1752.
    • (2004) Acta. Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1747-1752
    • Banaszak, K.1    Mechin, I.2
  • 10
    • 0027475212 scopus 로고
    • A pathway for disulfide bond formation in vivo
    • Bardwell J.C., Lee J.O., et al. A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA 1993, 90:1038-1042.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1038-1042
    • Bardwell, J.C.1    Lee, J.O.2
  • 11
    • 0027465807 scopus 로고
    • Disulfide bonding patterns and protein topologies
    • Benham C.J., Jafri M.S. Disulfide bonding patterns and protein topologies. Protein Sci. 1993, 2:41-54.
    • (1993) Protein Sci. , vol.2 , pp. 41-54
    • Benham, C.J.1    Jafri, M.S.2
  • 12
    • 15744375548 scopus 로고    scopus 로고
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC
    • Berkmen M., Boyd D., et al. The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J. Biol. Chem. 2005, 280:11387-11394.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2
  • 13
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette P.H., Aslund F., et al. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 1999, 96:13703-13708.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2
  • 14
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • Bessette P.H., Cotto J.J., et al. In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J. Biol. Chem. 1999, 274:7784-7792.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7784-7792
    • Bessette, P.H.1    Cotto, J.J.2
  • 15
    • 4644249680 scopus 로고    scopus 로고
    • Complete nucleotide sequence of a 92-kilobase plasmid harboring the CTX-M-15 extended-spectrum beta-lactamase involved in an outbreak in long-term-care facilities in Toronto, Canada
    • Boyd D.A., Tyler S, et al. Complete nucleotide sequence of a 92-kilobase plasmid harboring the CTX-M-15 extended-spectrum beta-lactamase involved in an outbreak in long-term-care facilities in Toronto, Canada. Antimicrob. Agents Chemother. 2004, 48:3758-3764.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3758-3764
    • Boyd, D.A.1    Tyler, S.2
  • 16
    • 38049144593 scopus 로고    scopus 로고
    • Transfer of megaplasmid pKB1 from the rubber-degrading bacterium Gordonia westfalica strain Kb1 to related bacteria and its modification
    • Bröker D., Arenskötter M., et al. Transfer of megaplasmid pKB1 from the rubber-degrading bacterium Gordonia westfalica strain Kb1 to related bacteria and its modification. Appl. Microbiol. Biotechnol. 2008, 77:1317-1327.
    • (2008) Appl. Microbiol. Biotechnol. , vol.77 , pp. 1317-1327
    • Bröker, D.1    Arenskötter, M.2
  • 18
    • 0015419145 scopus 로고
    • Transfer among Erwinia spp. and other enterobacteria of antibiotic resistance carried on R factors
    • Chatterjee A.K., Starr M.P. Transfer among Erwinia spp. and other enterobacteria of antibiotic resistance carried on R factors. J. Bacteriol. 1972, 112:576-584.
    • (1972) J. Bacteriol. , vol.112 , pp. 576-584
    • Chatterjee, A.K.1    Starr, M.P.2
  • 19
    • 0033538564 scopus 로고    scopus 로고
    • Chaperone activity of DsbC
    • Chen J., Song J., et al. Chaperone activity of DsbC. J. Biol. Chem. 1999, 274:19601.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19601
    • Chen, J.1    Song, J.2
  • 20
    • 10744231052 scopus 로고    scopus 로고
    • Comparative genome analysis of Vibrio vulnificus, a marine pathogen
    • Chen C.Y., Wu K.M., et al. Comparative genome analysis of Vibrio vulnificus, a marine pathogen. Genome Res. 2003, 13:2577-2587.
    • (2003) Genome Res. , vol.13 , pp. 2577-2587
    • Chen, C.Y.1    Wu, K.M.2
  • 21
    • 34547632382 scopus 로고    scopus 로고
    • Sequencing and comparative genomic analysis of pK29, a 269-kilobase conjugative plasmid encoding CMY-8 and CTX-M-3 beta-lactamases in Klebsiella pneumoniae
    • Chen Y.T., Lauderdale T.L., et al. Sequencing and comparative genomic analysis of pK29, a 269-kilobase conjugative plasmid encoding CMY-8 and CTX-M-3 beta-lactamases in Klebsiella pneumoniae. Antimicrob. Agents Chemother. 2007, 51:3004-3007.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3004-3007
    • Chen, Y.T.1    Lauderdale, T.L.2
  • 22
    • 84881024411 scopus 로고    scopus 로고
    • Many roles of the bacterial envelope reducing pathways, Antiox Redox Signal. Epub ahead of print.
    • Cho, S., Collet, J.-F., 2012. Many roles of the bacterial envelope reducing pathways. Antiox Redox Signal. Epub ahead of print.
    • (2012)
    • Cho, S.1    Collet, J.-F.2
  • 23
    • 84860534459 scopus 로고    scopus 로고
    • A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope
    • Cho S., Parsonage D., et al. A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope. mBio 2012, 3:e00291-11.
    • (2012) mBio , vol.3
    • Cho, S.1    Parsonage, D.2
  • 24
    • 34547764270 scopus 로고    scopus 로고
    • Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility
    • Cho S.-H.H., Porat A., et al. Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility. EMBO J. 2007, 26:3509-3520.
    • (2007) EMBO J. , vol.26 , pp. 3509-3520
    • Cho, S.-H.H.1    Porat, A.2
  • 25
    • 0015410064 scopus 로고
    • R factors from Proteus rettgeri
    • Coetzee J.N., Datta N., et al. R factors from Proteus rettgeri. J. Gen. Microbiol. 1972, 72:543-552.
    • (1972) J. Gen. Microbiol. , vol.72 , pp. 543-552
    • Coetzee, J.N.1    Datta, N.2
  • 26
    • 0014457512 scopus 로고
    • Bacterial conjugation
    • Curtiss R. Bacterial conjugation. Annu. Rev. Microbiol. 1969, 23:69-136.
    • (1969) Annu. Rev. Microbiol. , vol.23 , pp. 69-136
    • Curtiss, R.1
  • 27
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • Darby N.J., Creighton T.E. Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry 1995, 34:3576-3587.
    • (1995) Biochemistry , vol.34 , pp. 3576-3587
    • Darby, N.J.1    Creighton, T.E.2
  • 28
    • 0032548471 scopus 로고    scopus 로고
    • Contributions of substrate binding to the catalytic activity of DsbC
    • Darby N.J., Raina S., et al. Contributions of substrate binding to the catalytic activity of DsbC. Biochemistry 1998, 37:783-791.
    • (1998) Biochemistry , vol.37 , pp. 783-791
    • Darby, N.J.1    Raina, S.2
  • 29
    • 70450160847 scopus 로고    scopus 로고
    • A periplasmic reducing system protects single cysteine residues from oxidation
    • Depuydt M., Leonard S.E., et al. A periplasmic reducing system protects single cysteine residues from oxidation. Science 2009, 326:1109-1111.
    • (2009) Science , vol.326 , pp. 1109-1111
    • Depuydt, M.1    Leonard, S.E.2
  • 30
    • 34848835185 scopus 로고    scopus 로고
    • A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c
    • Di Matteo A., Gianni S., et al. A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c. J. Biol. Chem. 2007, 282:27012-27019.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27012-27019
    • Di Matteo, A.1    Gianni, S.2
  • 31
    • 79954444578 scopus 로고    scopus 로고
    • Tracking F plasmid TraI relaxase processing reactions provides insight into F plasmid transfer
    • Dostál L., Shao S., et al. Tracking F plasmid TraI relaxase processing reactions provides insight into F plasmid transfer. Nucleic Acids Res. 2011, 39:2658-2670.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2658-2670
    • Dostál, L.1    Shao, S.2
  • 32
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Dutton R.J., Boyd D., et al. Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc. Natl. Acad. Sci. USA 2008, 105:11933-11938.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2
  • 33
    • 0036069067 scopus 로고    scopus 로고
    • Structure of CcmG/DsbE at 1.14A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment
    • Edeling M.A., Guddat L.W., et al. Structure of CcmG/DsbE at 1.14A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment. Structure 2002, 10:973-979.
    • (2002) Structure , vol.10 , pp. 973-979
    • Edeling, M.A.1    Guddat, L.W.2
  • 34
    • 28844446587 scopus 로고    scopus 로고
    • F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues
    • Elton T.C., Holland S.J., et al. F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues. J. Bacteriol. 2005, 187:8267-8277.
    • (2005) J. Bacteriol. , vol.187 , pp. 8267-8277
    • Elton, T.C.1    Holland, S.J.2
  • 35
    • 0031919407 scopus 로고    scopus 로고
    • The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo
    • Fabianek R.A., Hennecke H., et al. The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo. J. Bacteriol. 1998, 180:1947-1950.
    • (1998) J. Bacteriol. , vol.180 , pp. 1947-1950
    • Fabianek, R.A.1    Hennecke, H.2
  • 36
    • 0033032598 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation
    • Fabianek R.A., Hofer T., et al. Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation. Arch. Microbiol. 1999, 171:92-100.
    • (1999) Arch. Microbiol. , vol.171 , pp. 92-100
    • Fabianek, R.A.1    Hofer, T.2
  • 37
    • 0010405263 scopus 로고
    • Episomic element in a strain of Salmonella Typhosa
    • Falkow S., Baron L.S. Episomic element in a strain of Salmonella Typhosa. J. Bacteriol. 1962, 84:581-589.
    • (1962) J. Bacteriol. , vol.84 , pp. 581-589
    • Falkow, S.1    Baron, L.S.2
  • 39
    • 0036784622 scopus 로고    scopus 로고
    • CxxS: fold-independent redox motif revealed by genome-wide searches for thiol/disulfide oxidoreductase function
    • Fomenko D.E., Gladyshev V.N. CxxS: fold-independent redox motif revealed by genome-wide searches for thiol/disulfide oxidoreductase function. Prot. Sci. 2002, 11:2285-2296.
    • (2002) Prot. Sci. , vol.11 , pp. 2285-2296
    • Fomenko, D.E.1    Gladyshev, V.N.2
  • 40
    • 0141679346 scopus 로고    scopus 로고
    • Identity and functions of CxxC-derived motifs
    • Fomenko D.E., Gladyshev V.N. Identity and functions of CxxC-derived motifs. Biochemistry 2003, 38:11214-11225.
    • (2003) Biochemistry , vol.38 , pp. 11214-11225
    • Fomenko, D.E.1    Gladyshev, V.N.2
  • 41
    • 0028335140 scopus 로고
    • Analysis of the sequence and gene products of the transfer region of the F sex factor
    • Frost L.S., Ippen-Ihler K., et al. Analysis of the sequence and gene products of the transfer region of the F sex factor. Microbiol. Rev. 1994, 58:162-210.
    • (1994) Microbiol. Rev. , vol.58 , pp. 162-210
    • Frost, L.S.1    Ippen-Ihler, K.2
  • 42
    • 0021138993 scopus 로고
    • Physical and genetic analyses of the Inc-I alpha plasmid R64
    • Furuichi T., Komano T., et al. Physical and genetic analyses of the Inc-I alpha plasmid R64. J. Bacteriol. 1984, 158:997-1004.
    • (1984) J. Bacteriol. , vol.158 , pp. 997-1004
    • Furuichi, T.1    Komano, T.2
  • 43
    • 64349087867 scopus 로고    scopus 로고
    • The diversity of conjugative relaxases and its application in plasmid classification
    • Garcillán-Barcia M.P., Francia M.V., et al. The diversity of conjugative relaxases and its application in plasmid classification. FEMS Microbiol. Rev. 2009, 33:657-687.
    • (2009) FEMS Microbiol. Rev. , vol.33 , pp. 657-687
    • Garcillán-Barcia, M.P.1    Francia, M.V.2
  • 44
    • 0031979177 scopus 로고    scopus 로고
    • Cefotaxime-resistant enterobacteriaceae isolates from a hospital in Warsaw, Poland: identification of a new CTX-M-3 cefotaxime-hydrolyzing beta-lactamase that is closely related to the CTX-M-1/MEN-1 enzyme
    • Gniadkowski M., Schneider I., et al. Cefotaxime-resistant enterobacteriaceae isolates from a hospital in Warsaw, Poland: identification of a new CTX-M-3 cefotaxime-hydrolyzing beta-lactamase that is closely related to the CTX-M-1/MEN-1 enzyme. Antimicrob. Agents Chemother. 1998, 42:827-832.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 827-832
    • Gniadkowski, M.1    Schneider, I.2
  • 45
    • 0035859924 scopus 로고    scopus 로고
    • DsbC activation by the N-terminal domain of DsbD
    • Goldstone D., Haebel P.W., et al. DsbC activation by the N-terminal domain of DsbD. Proc. Natl. Acad. Sci. USA 2001, 98:9551-9556.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9551-9556
    • Goldstone, D.1    Haebel, P.W.2
  • 46
    • 0036217298 scopus 로고    scopus 로고
    • Structure and role of coupling proteins in conjugal DNA transfer
    • Gomis-Rüth F.X., De la Cruz F., et al. Structure and role of coupling proteins in conjugal DNA transfer. Res. Microbiol. 2002, 153:199-204.
    • (2002) Res. Microbiol. , vol.153 , pp. 199-204
    • Gomis-Rüth, F.X.1    De la Cruz, F.2
  • 47
    • 0027185234 scopus 로고
    • Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase
    • Gupta S.D., Gan M.B., et al. Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase. J. Biol. Chem. 1993, 268:16551-16556.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16551-16556
    • Gupta, S.D.1    Gan, M.B.2
  • 48
    • 0037119945 scopus 로고    scopus 로고
    • The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex
    • Haebel P.W., Goldstone D., et al. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex. EMBO J. 2002, 21:4774-4784.
    • (2002) EMBO J. , vol.21 , pp. 4774-4784
    • Haebel, P.W.1    Goldstone, D.2
  • 49
    • 0036363570 scopus 로고    scopus 로고
    • Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins
    • Hamann M., Zhang T., et al. Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins. Methods Enzymol. 2002, 348:146-156.
    • (2002) Methods Enzymol. , vol.348 , pp. 146-156
    • Hamann, M.1    Zhang, T.2
  • 50
    • 3843054585 scopus 로고    scopus 로고
    • Tra proteins characteristic of F-like type IV secretion systems constitute an interaction group by yeast two-hybrid analysis
    • Harris R.L., Silverman P.M. Tra proteins characteristic of F-like type IV secretion systems constitute an interaction group by yeast two-hybrid analysis. J. Bacteriol. 2004, 186:5480-5485.
    • (2004) J. Bacteriol. , vol.186 , pp. 5480-5485
    • Harris, R.L.1    Silverman, P.M.2
  • 52
    • 0017879413 scopus 로고
    • Cell-cell interactions in conjugating Escherichia coli: purification of F pili with biological activity
    • Helmuth R., Achtman M. Cell-cell interactions in conjugating Escherichia coli: purification of F pili with biological activity. Proc. Natl. Acad. Sci. USA 1978, 75:1237-1241.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1237-1241
    • Helmuth, R.1    Achtman, M.2
  • 53
    • 80052536012 scopus 로고    scopus 로고
    • TrbB from conjugative plasmid F Is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance
    • Hemmis C.W., Berkmen M., et al. TrbB from conjugative plasmid F Is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance. J. Bacteriol. 2011, 193:4588-4597.
    • (2011) J. Bacteriol. , vol.193 , pp. 4588-4597
    • Hemmis, C.W.1    Berkmen, M.2
  • 54
    • 0027511108 scopus 로고
    • Cloning and sequencing of Coxiella burnetii outer membrane protein gene com1
    • Hendrix L.R., Mallavia L.P., et al. Cloning and sequencing of Coxiella burnetii outer membrane protein gene com1. Infect. Immun. 1993, 61:470-477.
    • (1993) Infect. Immun. , vol.61 , pp. 470-477
    • Hendrix, L.R.1    Mallavia, L.P.2
  • 55
    • 2942669907 scopus 로고    scopus 로고
    • Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide
    • Heras B., Edeling M.A., et al. Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. Proc. Natl. Acad. Sci. USA 2004, 101:8876-8881.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8876-8881
    • Heras, B.1    Edeling, M.A.2
  • 56
    • 0037431958 scopus 로고    scopus 로고
    • Disulfide bond isomerization in prokaryotes
    • Hiniker A., Bardwell J.C.A. Disulfide bond isomerization in prokaryotes. Biochemistry 2003, 42:1179-1185.
    • (2003) Biochemistry , vol.42 , pp. 1179-1185
    • Hiniker, A.1    Bardwell, J.C.A.2
  • 57
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • Hiniker A., Bardwell J.C.A. In vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem. 2004, 279:12967-12973.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.C.A.2
  • 58
    • 26644437700 scopus 로고    scopus 로고
    • Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC
    • Hiniker A., Collet J.-F.F., et al. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J. Biol. Chem. 2005, 280:33785-33791.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33785-33791
    • Hiniker, A.1    Collet, J.-F.F.2
  • 59
    • 77949601825 scopus 로고    scopus 로고
    • CD-HIT suite: a web server for clustering and comparing biological sequences
    • Huang Y., Niu B., et al. CD-HIT suite: a web server for clustering and comparing biological sequences. Bioinformatics 2010, 26:680-682.
    • (2010) Bioinformatics , vol.26 , pp. 680-682
    • Huang, Y.1    Niu, B.2
  • 60
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba K., Murakami S., et al. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 2006, 127:789-801.
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1    Murakami, S.2
  • 61
    • 79955000469 scopus 로고    scopus 로고
    • DsbA2 (27kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system
    • Jameson-Lee M., Garduño R.A., et al. DsbA2 (27kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system. Mol. Microbiol. 2011, 80:835-852.
    • (2011) Mol. Microbiol. , vol.80 , pp. 835-852
    • Jameson-Lee, M.1    Garduño, R.A.2
  • 62
    • 39549104498 scopus 로고    scopus 로고
    • Comparative analysis of eight arthrobacter plasmids
    • Jerke K., Nakatsu C.H., et al. Comparative analysis of eight arthrobacter plasmids. Plasmid 2008, 59:73-85.
    • (2008) Plasmid , vol.59 , pp. 73-85
    • Jerke, K.1    Nakatsu, C.H.2
  • 63
    • 0035992095 scopus 로고    scopus 로고
    • Location of increased serum survival gene and selected virulence traits on a conjugative R plasmid in an avian Escherichia coli isolate
    • Johnson T.J., Giddings C.W., et al. Location of increased serum survival gene and selected virulence traits on a conjugative R plasmid in an avian Escherichia coli isolate. Avian Dis. 2002, 46:342-352.
    • (2002) Avian Dis. , vol.46 , pp. 342-352
    • Johnson, T.J.1    Giddings, C.W.2
  • 64
    • 33748663761 scopus 로고    scopus 로고
    • Complete DNA sequence of a ColBM plasmid from avian pathogenic Escherichia coli suggests that it evolved from closely related ColV virulence plasmids
    • Johnson T.J., Johnson S.J., et al. Complete DNA sequence of a ColBM plasmid from avian pathogenic Escherichia coli suggests that it evolved from closely related ColV virulence plasmids. J. Bacteriol. 2006, 188:5975-5983.
    • (2006) J. Bacteriol. , vol.188 , pp. 5975-5983
    • Johnson, T.J.1    Johnson, S.J.2
  • 65
    • 0041341888 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-negative bacteria
    • Juncker A.S., Willenbrock H., et al. Prediction of lipoprotein signal peptides in Gram-negative bacteria. Prot. Sci. 2003, 12:1652-1662.
    • (2003) Prot. Sci. , vol.12 , pp. 1652-1662
    • Juncker, A.S.1    Willenbrock, H.2
  • 66
    • 0025880609 scopus 로고
    • Construction and characterization of derivatives carrying insertion mutations in F plasmid transfer region genes, trbA, artA, traQ, and trbB
    • Kathir P., Ippen-Ihler K. Construction and characterization of derivatives carrying insertion mutations in F plasmid transfer region genes, trbA, artA, traQ, and trbB. Plasmid 1991, 26:40-54.
    • (1991) Plasmid , vol.26 , pp. 40-54
    • Kathir, P.1    Ippen-Ihler, K.2
  • 67
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen F., Beckwith J. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 2000, 103:769-779.
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 68
    • 0042838288 scopus 로고    scopus 로고
    • Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD
    • Katzen F., Beckwith J. Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. Proc. Natl. Acad. Sci. USA 2003, 100:10471-10476.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10471-10476
    • Katzen, F.1    Beckwith, J.2
  • 69
    • 0001880535 scopus 로고
    • Relative probabilities of isomers in cystine-containing randomly coiled polypeptides
    • Academic Press, New York, R. Benesch, R.E. Benesch, P. Boyer, I. Klotz, W.R. Middlebrook, A. Szent-Gyorgyi, D.R. Schwarz (Eds.)
    • Kauzmann W. Relative probabilities of isomers in cystine-containing randomly coiled polypeptides. Sulfur in Proteins 1959, 93-108. Academic Press, New York. R. Benesch, R.E. Benesch, P. Boyer, I. Klotz, W.R. Middlebrook, A. Szent-Gyorgyi, D.R. Schwarz (Eds.).
    • (1959) Sulfur in Proteins , pp. 93-108
    • Kauzmann, W.1
  • 70
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley L.A., Sternberg M.J.E. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 71
    • 38649107060 scopus 로고    scopus 로고
    • Complete DNA sequence and analysis of the transferable multiple-drug resistance plasmids (R Plasmids) from Photobacterium damselae subsp. Piscicida isolates collected in Japan and the United States
    • Kim M.J., Hirono I., et al. Complete DNA sequence and analysis of the transferable multiple-drug resistance plasmids (R Plasmids) from Photobacterium damselae subsp. Piscicida isolates collected in Japan and the United States. Antimicrob. Agents Chemother. 2008, 52:606-611.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 606-611
    • Kim, M.J.1    Hirono, I.2
  • 72
    • 0033106153 scopus 로고    scopus 로고
    • Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
    • Kobayashi T., Ito K. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. EMBO J. 1999, 18:1192-1198.
    • (1999) EMBO J. , vol.18 , pp. 1192-1198
    • Kobayashi, T.1    Ito, K.2
  • 73
    • 0030671552 scopus 로고    scopus 로고
    • Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
    • Kobayashi T., Kishigami S., et al. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. Proc. Natl. Acad. Sci. USA 1997, 94:11857-11862.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11857-11862
    • Kobayashi, T.1    Kishigami, S.2
  • 74
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin M.A., Blackshields G., et al. Clustal W and Clustal X version 2.0. Bioinformatics 2007, 23:2947-2948.
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1    Blackshields, G.2
  • 75
    • 0038308165 scopus 로고    scopus 로고
    • F factor conjugation is a true type IV secretion system
    • Lawley T.D., Klimke W.A., et al. F factor conjugation is a true type IV secretion system. FEMS Microbiol. Lett. 2003, 224:1-15.
    • (2003) FEMS Microbiol. Lett. , vol.224 , pp. 1-15
    • Lawley, T.D.1    Klimke, W.A.2
  • 76
    • 0000006747 scopus 로고
    • Sex compatibility in Escherichia coli
    • Lederberg J., Cavalli L.L. Sex compatibility in Escherichia coli. Genetics 1952, 37:720-730.
    • (1952) Genetics , vol.37 , pp. 720-730
    • Lederberg, J.1    Cavalli, L.L.2
  • 77
    • 39749085184 scopus 로고    scopus 로고
    • A common virulence plasmid in biotype 2 Vibrio vulnificus and its dissemination aided by a conjugal plasmid
    • Lee C.T., Amaro C.C., et al. A common virulence plasmid in biotype 2 Vibrio vulnificus and its dissemination aided by a conjugal plasmid. J. Bacteriol. 2008, 190:1638-1648.
    • (2008) J. Bacteriol. , vol.190 , pp. 1638-1648
    • Lee, C.T.1    Amaro, C.C.2
  • 78
    • 0028021929 scopus 로고
    • Expression, purification, and functional properties of Bradyrhizobium japonicum TlpA, a thioredoxin-like protein
    • Loferer H., Hennecke H. Expression, purification, and functional properties of Bradyrhizobium japonicum TlpA, a thioredoxin-like protein. Eur. J. Biochem. 1995, 223:339-344.
    • (1995) Eur. J. Biochem. , vol.223 , pp. 339-344
    • Loferer, H.1    Hennecke, H.2
  • 79
    • 0027303321 scopus 로고
    • Bradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosis
    • Loferer H., Bott M., et al. Bradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosis. EMBO J. 1993, 12:3373-3383.
    • (1993) EMBO J. , vol.12 , pp. 3373-3383
    • Loferer, H.1    Bott, M.2
  • 80
    • 0028848166 scopus 로고
    • A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins
    • Loferer H., Wunderlich M., et al. A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins. J. Biol. Chem. 1995, 270:26178-26183.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26178-26183
    • Loferer, H.1    Wunderlich, M.2
  • 81
    • 0027216726 scopus 로고
    • Host range and transfer efficiency of incompatibility group HI plasmids
    • Maher D., Taylor D.E. Host range and transfer efficiency of incompatibility group HI plasmids. Can. J. Microbiol. 1993, 39:581-587.
    • (1993) Can. J. Microbiol. , vol.39 , pp. 581-587
    • Maher, D.1    Taylor, D.E.2
  • 82
    • 54549124476 scopus 로고    scopus 로고
    • Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
    • Malojcić G., Owen R.L., et al. Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB. FEBS Lett. 2008, 582:3301-3307.
    • (2008) FEBS Lett. , vol.582 , pp. 3301-3307
    • Malojcić, G.1    Owen, R.L.2
  • 83
    • 78651285748 scopus 로고    scopus 로고
    • CDD: a conserved domain database for the functional annotation of proteins
    • Marchler-Bauer A., Lu S., et al. CDD: a conserved domain database for the functional annotation of proteins. Nucleic Acids Res. 2011, 39:D225-D229.
    • (2011) Nucleic Acids Res. , vol.39
    • Marchler-Bauer, A.1    Lu, S.2
  • 84
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin J.L., Bardwell J.C., et al. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 1993, 365:464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2
  • 85
    • 0034048647 scopus 로고    scopus 로고
    • Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
    • McCarthy A.A., Haebel P.W., et al. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat. Struct. Biol. 2000, 7:196-199.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 196-199
    • McCarthy, A.A.1    Haebel, P.W.2
  • 86
    • 35748965031 scopus 로고    scopus 로고
    • The oxidase DsbA folds a protein with a nonconsecutive disulfide
    • Messens J., Collet J.-F., et al. The oxidase DsbA folds a protein with a nonconsecutive disulfide. J. Biol. Chem. 2007, 282:31302-31307.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31302-31307
    • Messens, J.1    Collet, J.-F.2
  • 88
    • 27644539245 scopus 로고    scopus 로고
    • AtCCMH, an essential component of the c-type cytochrome maturation pathway in Arabidopsis mitochondria, interacts with apocytochrome c
    • Meyer E.H., Giegé P., et al. AtCCMH, an essential component of the c-type cytochrome maturation pathway in Arabidopsis mitochondria, interacts with apocytochrome c. Proc. Natl. Acad. Sci. USA 2005, 102:16113-16118.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16113-16118
    • Meyer, E.H.1    Giegé, P.2
  • 89
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas D., Georgopoulos C., et al. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 1994, 13:2013-2020.
    • (1994) EMBO J. , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2
  • 90
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas D., Schwager F., et al. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 1995, 14:3415-3424.
    • (1995) EMBO J. , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2
  • 91
    • 8844270875 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
    • Nakamoto H., Bardwell J.C.A. Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim. Biophys. Acta 2004, 1694:111-119.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 111-119
    • Nakamoto, H.1    Bardwell, J.C.A.2
  • 92
  • 93
    • 0014250426 scopus 로고
    • Inhibition of bacterial conjugation by ribonucleic acid and deoxyribonucleic acid male-specific bacteriophages
    • Novotny C., Knight W.S., et al. Inhibition of bacterial conjugation by ribonucleic acid and deoxyribonucleic acid male-specific bacteriophages. J. Bacteriol. 1968, 95:314-326.
    • (1968) J. Bacteriol. , vol.95 , pp. 314-326
    • Novotny, C.1    Knight, W.S.2
  • 94
    • 0014800347 scopus 로고
    • Role of pili in bacterial conjugation
    • Ou J.T., Anderson T.F. Role of pili in bacterial conjugation. J. Bacteriol. 1970, 102:648-654.
    • (1970) J. Bacteriol. , vol.102 , pp. 648-654
    • Ou, J.T.1    Anderson, T.F.2
  • 95
    • 0037470983 scopus 로고    scopus 로고
    • Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis
    • Paulsen I.T., Banerjei L., et al. Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science 2003, 299:2071-2074.
    • (2003) Science , vol.299 , pp. 2071-2074
    • Paulsen, I.T.1    Banerjei, L.2
  • 96
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Peterson T.N., Brunak S., et al. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Peterson, T.N.1    Brunak, S.2
  • 98
    • 0023444994 scopus 로고
    • Organization and regulation of the conjugation genes of IncI1 plasmid colIb-P9
    • Rees C.E., Bradley D.E., et al. Organization and regulation of the conjugation genes of IncI1 plasmid colIb-P9. Plasmid 1987, 18:223-236.
    • (1987) Plasmid , vol.18 , pp. 223-236
    • Rees, C.E.1    Bradley, D.E.2
  • 99
    • 0037031882 scopus 로고    scopus 로고
    • DsbB catalyzes disulfide bond formation de novo
    • Regeimbal J., Bardwell J.C. DsbB catalyzes disulfide bond formation de novo. J. Biol. Chem. 2002, 277:32706-32713.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32706-32713
    • Regeimbal, J.1    Bardwell, J.C.2
  • 100
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch A., Belin D., et al. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. USA 1996, 93:13048-13053.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13048-13053
    • Rietsch, A.1    Belin, D.2
  • 101
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch A., Bessette P., et al. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 1997, 179:6602-6608.
    • (1997) J. Bacteriol. , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2
  • 102
    • 0033027259 scopus 로고    scopus 로고
    • Complete sequence of a 184-kilobase catabolic plasmid from Sphingomonas aromaticivorans F199
    • Romine M.F., Stillwell L.C., et al. Complete sequence of a 184-kilobase catabolic plasmid from Sphingomonas aromaticivorans F199. J. Bacteriol. 1999, 181:1585-1602.
    • (1999) J. Bacteriol. , vol.181 , pp. 1585-1602
    • Romine, M.F.1    Stillwell, L.C.2
  • 103
    • 2442607486 scopus 로고    scopus 로고
    • Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD
    • Rozhkova A., Stirnimann C.U., et al. Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. EMBO J. 2004, 23:1709-1719.
    • (2004) EMBO J. , vol.23 , pp. 1709-1719
    • Rozhkova, A.1    Stirnimann, C.U.2
  • 104
    • 0000972208 scopus 로고
    • The reformation of disulfide bridges in proteins
    • Sela M., Lifson S. The reformation of disulfide bridges in proteins. Biochim. Biophys. Acta 1959, 36:471-478.
    • (1959) Biochim. Biophys. Acta , vol.36 , pp. 471-478
    • Sela, M.1    Lifson, S.2
  • 105
    • 0034607656 scopus 로고    scopus 로고
    • DsbG, a protein disulfide isomerase with chaperone activity
    • Shao F., Bader M.W., et al. DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem. 2000, 275:13349-13352.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13349-13352
    • Shao, F.1    Bader, M.W.2
  • 106
    • 0034657620 scopus 로고    scopus 로고
    • The complete DNA sequence and analysis of R27, a large IncHI plasmid from Salmonella typhi that is temperature sensitive for transfer
    • Sherburne C.K., Lawley T.D., et al. The complete DNA sequence and analysis of R27, a large IncHI plasmid from Salmonella typhi that is temperature sensitive for transfer. Nucleic Acids Res. 2000, 28:2177-2186.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2177-2186
    • Sherburne, C.K.1    Lawley, T.D.2
  • 107
    • 0028063372 scopus 로고
    • Escherichia coli DNA helicase I catalyzes a sequence-specific cleavage/ligation reaction at the F plasmid origin of transfer
    • Sherman J.A., Matson S.W. Escherichia coli DNA helicase I catalyzes a sequence-specific cleavage/ligation reaction at the F plasmid origin of transfer. J. Biol. Chem. 1994, 269:26220-26226.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26220-26226
    • Sherman, J.A.1    Matson, S.W.2
  • 108
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik V.E., Condemine G., et al. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 1994, 13:2007-2012.
    • (1994) EMBO J. , vol.13 , pp. 2007-2012
    • Shevchik, V.E.1    Condemine, G.2
  • 109
    • 33646588646 scopus 로고    scopus 로고
    • Characterization of the replication, maintenance, and transfer features of the IncP-7 plasmid pCAR1, which carries genes involved in carbazole and dioxin degradation
    • Shintani M., Yano H., et al. Characterization of the replication, maintenance, and transfer features of the IncP-7 plasmid pCAR1, which carries genes involved in carbazole and dioxin degradation. Appl. Environ. Microbiol. 2006, 72:3206-3216.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3206-3216
    • Shintani, M.1    Yano, H.2
  • 110
    • 72949101778 scopus 로고    scopus 로고
    • In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling
    • Shouldice S.R., Cho S.-H.H., et al. In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling. Mol. Microbiol. 2010, 75:13-28.
    • (2010) Mol. Microbiol. , vol.75 , pp. 13-28
    • Shouldice, S.R.1    Cho, S.-H.H.2
  • 111
    • 33750438800 scopus 로고    scopus 로고
    • Acquisition of avian pathogenic Escherichia coli plasmids by a commensal E. coli isolate enhances its abilities to kill chicken embryos, grow in human urine, and colonize the murine kidney
    • Skyberg J.A., Johnson T.J., et al. Acquisition of avian pathogenic Escherichia coli plasmids by a commensal E. coli isolate enhances its abilities to kill chicken embryos, grow in human urine, and colonize the murine kidney. Infect. Immun. 2006, 74:6287-6292.
    • (2006) Infect. Immun. , vol.74 , pp. 6287-6292
    • Skyberg, J.A.1    Johnson, T.J.2
  • 113
    • 80255122757 scopus 로고    scopus 로고
    • Cytochrome c biogenesis system I
    • Stevens J.M., Mavridou D.A., et al. Cytochrome c biogenesis system I. FEBS J. 2011, 278:4170-4178.
    • (2011) FEBS J. , vol.278 , pp. 4170-4178
    • Stevens, J.M.1    Mavridou, D.A.2
  • 114
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • Stewart E.J., Katzen F., et al. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. EMBO J. 1999, 18:5963-5971.
    • (1999) EMBO J. , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2
  • 115
    • 21744448514 scopus 로고    scopus 로고
    • Structural basis and kinetics of DsbD-dependent cytochrome c maturation
    • Stirnimann C.U., Rozhkova A., et al. Structural basis and kinetics of DsbD-dependent cytochrome c maturation. Structure 2005, 13:985-993.
    • (2005) Structure , vol.13 , pp. 985-993
    • Stirnimann, C.U.1    Rozhkova, A.2
  • 116
    • 0034725691 scopus 로고    scopus 로고
    • The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC
    • Sun X.X., Wang C.C. The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC. J. Biol. Chem. 2000, 275:22743-22749.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22743-22749
    • Sun, X.X.1    Wang, C.C.2
  • 117
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., et al. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2
  • 118
    • 65449152830 scopus 로고    scopus 로고
    • Inactivation of thioredoxin-like gene alters oxidative stress resistance and reduces cytochrome c oxidase activity in Agrobacterium tumefaciens
    • Tanboon W., Chuchue T., et al. Inactivation of thioredoxin-like gene alters oxidative stress resistance and reduces cytochrome c oxidase activity in Agrobacterium tumefaciens. FEMS Microbiol. Lett. 2009, 295:110-116.
    • (2009) FEMS Microbiol. Lett. , vol.295 , pp. 110-116
    • Tanboon, W.1    Chuchue, T.2
  • 119
    • 0014127307 scopus 로고
    • Thermosensitive replication of a kanamycin resistance factor
    • Terawaki Y., Takayasu H., et al. Thermosensitive replication of a kanamycin resistance factor. J. Bacteriol. 1967, 94:687-690.
    • (1967) J. Bacteriol. , vol.94 , pp. 687-690
    • Terawaki, Y.1    Takayasu, H.2
  • 120
    • 0012295404 scopus 로고
    • Post-translational modification and processing of Escherichia coli prolipoprotein in vitro
    • Tokunga M., Tokunga H., Wu H.C. Post-translational modification and processing of Escherichia coli prolipoprotein in vitro. PNAS 1982, 79:2255-2259.
    • (1982) PNAS , vol.79 , pp. 2255-2259
    • Tokunga, M.1    Tokunga, H.2    Wu, H.C.3
  • 121
    • 53849121947 scopus 로고    scopus 로고
    • Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation
    • Turkarslan S., Sanders C., et al. Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation. Mol. Microbiol. 2008, 70:652-666.
    • (2008) Mol. Microbiol. , vol.70 , pp. 652-666
    • Turkarslan, S.1    Sanders, C.2
  • 122
    • 15444375047 scopus 로고    scopus 로고
    • Functional analysis of three plasmids from Lactobacillus plantarum
    • van Kranenburg R., Golic N., et al. Functional analysis of three plasmids from Lactobacillus plantarum. Appl. Environ. Microbiol. 2005, 71:1223-1230.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1223-1230
    • van Kranenburg, R.1    Golic, N.2
  • 123
    • 0041923644 scopus 로고    scopus 로고
    • Molecular analysis of incHI1 antimicrobial resistance plasmids from Salmonella serovar Typhi strains associated with typhoid fever
    • Wain J., DiemNga L.T., et al. Molecular analysis of incHI1 antimicrobial resistance plasmids from Salmonella serovar Typhi strains associated with typhoid fever. Antimicrob. Agents Chemother. 2003, 47:2732-2739.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2732-2739
    • Wain, J.1    DiemNga, L.T.2
  • 124
    • 54049099392 scopus 로고    scopus 로고
    • Multiple antimicrobial resistance in plague: an emerging public health risk
    • Welch T.J., Fricke W.F., et al. Multiple antimicrobial resistance in plague: an emerging public health risk. PLoS One 2007, 2:e309.
    • (2007) PLoS One , vol.2
    • Welch, T.J.1    Fricke, W.F.2
  • 125
    • 0023370122 scopus 로고
    • Analysis of Escherichia coli K12 F factor transfer genes: traQ, trbA, and trbB
    • Wu J.H., Moore D., et al. Analysis of Escherichia coli K12 F factor transfer genes: traQ, trbA, and trbB. Plasmid 1987, 18:54-69.
    • (1987) Plasmid , vol.18 , pp. 54-69
    • Wu, J.H.1    Moore, D.2
  • 126
    • 0023688844 scopus 로고
    • The product of the F plasmid transfer operon gene, traF, is a periplasmic protein
    • Wu J.H., Kathir P., et al. The product of the F plasmid transfer operon gene, traF, is a periplasmic protein. J. Bacteriol. 1988, 170:3633-3639.
    • (1988) J. Bacteriol. , vol.170 , pp. 3633-3639
    • Wu, J.H.1    Kathir, P.2
  • 127
    • 0027366182 scopus 로고
    • Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH
    • Wunderlich M., Otto A., et al. Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH. Biochemistry 1993, 32:12251-12256.
    • (1993) Biochemistry , vol.32 , pp. 12251-12256
    • Wunderlich, M.1    Otto, A.2
  • 128
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun A., Missiakas D., et al. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 1995, 34:5075-5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2
  • 130
    • 84858223937 scopus 로고    scopus 로고
    • Assembly and mechanisms of bacterial type IV secretion machines
    • Zechner E.L., Lang S., et al. Assembly and mechanisms of bacterial type IV secretion machines. Philos. Trans. R. Soc. London, B 2012, 367:1073-1087.
    • (2012) Philos. Trans. R. Soc. London, B , vol.367 , pp. 1073-1087
    • Zechner, E.L.1    Lang, S.2
  • 131
    • 0242353305 scopus 로고    scopus 로고
    • Dimerization by domain hybridization bestows chaperone and isomerase activities
    • Zhao Z., Peng Y., et al. Dimerization by domain hybridization bestows chaperone and isomerase activities. J. Biol. Chem. 2003, 278:43292-43298.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43292-43298
    • Zhao, Z.1    Peng, Y.2
  • 132
    • 52049098074 scopus 로고    scopus 로고
    • NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation
    • Zhou Y., Cierpicki T., et al. NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation. Mol. Cell 2008, 31:896-908.
    • (2008) Mol. Cell , vol.31 , pp. 896-908
    • Zhou, Y.1    Cierpicki, T.2
  • 133
    • 34247122644 scopus 로고    scopus 로고
    • Mosaic structure of p1658/97, a 125-kilobase plasmid harboring an active amplicon with the extended-spectrum beta-lactamase gene blaSHV-5
    • Zienkiewicz M., Kern.-Zdanowicz I., et al. Mosaic structure of p1658/97, a 125-kilobase plasmid harboring an active amplicon with the extended-spectrum beta-lactamase gene blaSHV-5. Antimicrob. Agents Chemother. 2007, 51:1164-1171.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 1164-1171
    • Zienkiewicz, M.1    Kern-Zdanowicz, I.2


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