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Volumn 160, Issue PART 9, 2014, Pages 2053-2066

It takes two to tango: Two TatA paralogues and two redox enzyme-specific chaperones are involved in the localization of twin-arginine translocase substrates in Campylobacter jejuni

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; ARGININE; BACTERIAL ENZYME; CARRIER PROTEIN; CHAPERONE; FDHM PROTEIN; FLAVOPROTEIN; FORMATE DEHYDROGENASE; FUMARATE REDUCTASE; GLYCINE; METHYL MENAQUINONE FUMARATE REDUCTASE; MULTI COPPER OXIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NITRATE REDUCTASE; OXIDOREDUCTASE; PERIPLASMIC PROTEIN; PHENYLALANINE; SULFITE OXIDASE; TRIMETHYLAMINE OXIDE REDUCTASE; UNCLASSIFIED DRUG; ENZYME;

EID: 84906861173     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.080713-0     Document Type: Article
Times cited : (10)

References (73)
  • 1
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami, M., Lüke, I., Deitermann, S., Eisner, G., Koch, H. G., Brunner, J. & Müller, M. (2003). Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol Cell 12, 937-946.
    • (2003) Mol Cell , vol.12 , pp. 937-946
    • Alami, M.1    Lüke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.G.5    Brunner, J.6    Müller, M.7
  • 2
    • 84901650944 scopus 로고    scopus 로고
    • Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly
    • Aldridge, C., Ma, X., Gerard, F. & Cline, K. (2014). Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly. J Cell Biol 205, 51-65.
    • (2014) J Cell Biol , vol.205 , pp. 51-65
    • Aldridge, C.1    Ma, X.2    Gerard, F.3    Cline, K.4
  • 3
    • 33750077246 scopus 로고    scopus 로고
    • The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin-arginine translocase
    • Bachmann, J., Bauer, B., Zwicker, K., Ludwig, B. & Anderka, O. (2006). The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin-arginine translocase. FEBS J 273, 4817-4830.
    • (2006) FEBS J , vol.273 , pp. 4817-4830
    • Bachmann, J.1    Bauer, B.2    Zwicker, K.3    Ludwig, B.4    Anderka, O.5
  • 4
    • 84863229364 scopus 로고    scopus 로고
    • Structure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter
    • Baglieri, J., Beck, D., Vasisht, N., Smith, C. J. & Robinson, C. (2012). Structure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter. J Biol Chem 287, 7335-7344.
    • (2012) J Biol Chem , vol.287 , pp. 7335-7344
    • Baglieri, J.1    Beck, D.2    Vasisht, N.3    Smith, C.J.4    Robinson, C.5
  • 5
    • 2342596286 scopus 로고    scopus 로고
    • Topological studies on the twin-arginine translocase component TatC
    • Behrendt, J., Standar, K., Lindenstrauss, U. & Brüser, T. (2004). Topological studies on the twin-arginine translocase component TatC. FEMS Microbiol Lett 234, 303-308.
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 303-308
    • Behrendt, J.1    Standar, K.2    Lindenstrauss, U.3    Brüser, T.4
  • 7
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. C. (1996). A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22, 393-404.
    • (1996) Mol Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 8
    • 40749084835 scopus 로고    scopus 로고
    • Characterization of two putative cytochrome c peroxidases of Campylobacter jejuni involved in promoting commensal colonization of poultry
    • Bingham-Ramos, L. K. & Hendrixson, D. R. (2008). Characterization of two putative cytochrome c peroxidases of Campylobacter jejuni involved in promoting commensal colonization of poultry. Infect Immun 76, 1105-1114.
    • (2008) Infect Immun , vol.76 , pp. 1105-1114
    • Bingham-Ramos, L.K.1    Hendrixson, D.R.2
  • 9
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch, E. G., Sargent, F., Stanley, N. R., Berks, B. C., Robinson, C. & Palmer, T. (1998). An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem 273, 18003-18006.
    • (1998) J Biol Chem , vol.273 , pp. 18003-18006
    • Bogsch, E.G.1    Sargent, F.2    Stanley, N.R.3    Berks, B.C.4    Robinson, C.5    Palmer, T.6
  • 10
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twinarginine translocase fromEscherichia coli
    • Bolhuis, A., Mathers, J. E., Thomas, J. D., Barrett, C. M. & Robinson, C. (2001). TatB and TatC form a functional and structural unit of the twinarginine translocase fromEscherichia coli. J BiolChem276, 20213-20219.
    • (2001) J BiolChem , vol.276 , pp. 20213-20219
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.M.4    Robinson, C.5
  • 11
    • 80155164952 scopus 로고    scopus 로고
    • The Bdellovibrio bacteriovorus twin-arginine transport system has roles in predatory and prey-independent growth
    • Chang, C. Y., Hobley, L., Till, R., Capeness, M., Kanna, M., Burtt, W., Jagtap, P., Aizawa, S. & Sockett, R. E. (2011). The Bdellovibrio bacteriovorus twin-arginine transport system has roles in predatory and prey-independent growth. Microbiology 157, 3079-3093.
    • (2011) Microbiology , vol.157 , pp. 3079-3093
    • Chang, C.Y.1    Hobley, L.2    Till, R.3    Capeness, M.4    Kanna, M.5    Burtt, W.6    Jagtap, P.7    Aizawa, S.8    Sockett, R.E.9
  • 12
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • WEB SERVER ISSUE
    • Cole, C., Barber, J. D. & Barton, G. J. (2008). The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36 (Web Server issue), W197-201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 13
    • 84891829474 scopus 로고    scopus 로고
    • Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone
    • Dow, J. M., Grahl, S., Ward, R., Evans, R., Byron, O., Norman, D. G., Palmer, T. & Sargent, F. (2014). Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone. FEBS J 281, 246-260.
    • (2014) FEBS J , vol.281 , pp. 246-260
    • Dow, J.M.1    Grahl, S.2    Ward, R.3    Evans, R.4    Byron, O.5    Norman, D.G.6    Palmer, T.7    Sargent, F.8
  • 14
    • 84878482772 scopus 로고    scopus 로고
    • High-resolution transcriptome maps reveal strain-specific regulatory features of multiple Campylobacter jejuni isolates
    • Dugar, G., Herbig, A., Förstner, K. U., Heidrich, N., Reinhardt, R., Nieselt, K. & Sharma, C. M. (2013). High-resolution transcriptome maps reveal strain-specific regulatory features of multiple Campylobacter jejuni isolates. PLoS Genet 9, e1003495.
    • (2013) PLoS Genet , vol.9
    • Dugar, G.1    Herbig, A.2    Förstner, K.U.3    Heidrich, N.4    Reinhardt, R.5    Nieselt, K.6    Sharma, C.M.7
  • 15
    • 77957862665 scopus 로고    scopus 로고
    • The Campylobacter genetic toolbox: Development of tractable and generally applicable genetic techniques for Campylobacter jejuni
    • Gaskin, D. J. H., Van Vliet, A. H. M. & Pearson, B. M. (2007). The Campylobacter genetic toolbox: development of tractable and generally applicable genetic techniques for Campylobacter jejuni. Zoon Publ Health 54 (suppl. 1), 101.
    • (2007) Zoon Publ Health , vol.54 , Issue.SUPPL. 1 , pp. 101
    • Gaskin, D.J.H.1    Van Vliet, A.H.M.2    Pearson, B.M.3
  • 19
    • 34147125271 scopus 로고    scopus 로고
    • DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone
    • Graubner, W., Schierhorn, A. & Brüser, T. (2007). DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone. J Biol Chem 282, 7116-7124.
    • (2007) J Biol Chem , vol.282 , pp. 7116-7124
    • Graubner, W.1    Schierhorn, A.2    Brüser, T.3
  • 20
    • 34548208263 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis and disulfide mapping studies of the TatA component of the bacterial twin arginine translocase
    • Greene, N. P., Porcelli, I., Buchanan, G., Hicks, M. G., Schermann, S. M., Palmer, T. & Berks, B. C. (2007). Cysteine scanning mutagenesis and disulfide mapping studies of the TatA component of the bacterial twin arginine translocase. J Biol Chem 282, 23937-23945.
    • (2007) J Biol Chem , vol.282 , pp. 23937-23945
    • Greene, N.P.1    Porcelli, I.2    Buchanan, G.3    Hicks, M.G.4    Schermann, S.M.5    Palmer, T.6    Berks, B.C.7
  • 21
    • 77953943092 scopus 로고    scopus 로고
    • Reduction of fumarate, mesaconate and crotonate by Mfr, a novel oxygen-regulated periplasmic reductase in Campylobacter jejuni
    • Guccione, E., Hitchcock, A., Hall, S. J., Mulholland, F., Shearer, N., van Vliet, A. H. & Kelly, D. J. (2010). Reduction of fumarate, mesaconate and crotonate by Mfr, a novel oxygen-regulated periplasmic reductase in Campylobacter jejuni. Environ Microbiol 12, 576-591.
    • (2010) Environ Microbiol , vol.12 , pp. 576-591
    • Guccione, E.1    Hitchcock, A.2    Hall, S.J.3    Mulholland, F.4    Shearer, N.5    van Vliet, A.H.6    Kelly, D.J.7
  • 22
    • 57349087130 scopus 로고    scopus 로고
    • A multicopper oxidase (Cj1516) and a CopA homologue (Cj1161) are major components of the copper homeostasis system of Campylobacter jejuni
    • Hall, S. J., Hitchcock, A., Butler, C. S. & Kelly, D. J. (2008). A multicopper oxidase (Cj1516) and a CopA homologue (Cj1161) are major components of the copper homeostasis system of Campylobacter jejuni. J Bacteriol 190, 8075-8085.
    • (2008) J Bacteriol , vol.190 , pp. 8075-8085
    • Hall, S.J.1    Hitchcock, A.2    Butler, C.S.3    Kelly, D.J.4
  • 23
    • 0141789788 scopus 로고    scopus 로고
    • A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase
    • Hatzixanthis, K., Palmer, T. & Sargent, F. (2003). A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Mol Microbiol 49, 1377-1390.
    • (2003) Mol Microbiol , vol.49 , pp. 1377-1390
    • Hatzixanthis, K.1    Palmer, T.2    Sargent, F.3
  • 24
    • 0034745728 scopus 로고    scopus 로고
    • Role of the Tat transport system in nitrous oxide reductase translocation and cytochrome cd1 biosynthesis in Pseudomonas stutzeri
    • Heikkilä, M. P., Honisch, U., Wunsch, P. & Zumft, W. G. (2001). Role of the Tat transport system in nitrous oxide reductase translocation and cytochrome cd1 biosynthesis in Pseudomonas stutzeri. J Bacteriol 183, 1663-1671.
    • (2001) J Bacteriol , vol.183 , pp. 1663-1671
    • Heikkilä, M.P.1    Honisch, U.2    Wunsch, P.3    Zumft, W.G.4
  • 25
    • 0037468635 scopus 로고    scopus 로고
    • The Escherichia coli twin-arginine translocase: Conserved residues of TatA and TatB family components involved in protein transport
    • Hicks, M. G., de Leeuw, E., Porcelli, I., Buchanan, G., Berks, B. C. & Palmer, T. (2003). The Escherichia coli twin-arginine translocase: conserved residues of TatA and TatB family components involved in protein transport. FEBS Lett 539, 61-67.
    • (2003) FEBS Lett , vol.539 , pp. 61-67
    • Hicks, M.G.1    de Leeuw, E.2    Porcelli, I.3    Buchanan, G.4    Berks, B.C.5    Palmer, T.6
  • 26
    • 77957867732 scopus 로고    scopus 로고
    • Roles of the twin-arginine translocase and associated chaperones in the biogenesis of the electron transport chains of the human pathogen Campylobacter jejuni
    • Hitchcock, A., Hall, S. J., Myers, J. D., Mulholland, F., Jones, M. A. & Kelly, D. J. (2010). Roles of the twin-arginine translocase and associated chaperones in the biogenesis of the electron transport chains of the human pathogen Campylobacter jejuni. Microbiology 156, 2994-3010.
    • (2010) Microbiology , vol.156 , pp. 2994-3010
    • Hitchcock, A.1    Hall, S.J.2    Myers, J.D.3    Mulholland, F.4    Jones, M.A.5    Kelly, D.J.6
  • 27
    • 84861912744 scopus 로고    scopus 로고
    • Hydrogenase activity in the foodborne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikZYXWV) and is SlyD-independent
    • Howlett, R. M., Hughes, B. M., Hitchcock, A. & Kelly, D. J. (2012). Hydrogenase activity in the foodborne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikZYXWV) and is SlyD-independent. Microbiology 158, 1645-1655.
    • (2012) Microbiology , vol.158 , pp. 1645-1655
    • Howlett, R.M.1    Hughes, B.M.2    Hitchcock, A.3    Kelly, D.J.4
  • 28
    • 33846306363 scopus 로고    scopus 로고
    • Zantedeschia mild mosaic virus, a new widespread virus in calla lily, detected by ELISA, dot-blot hybridization and IC-RT-PCR
    • Huang, C.-H., Hu, W.-C., Yang, T.-C. & Chang, Y.-C. (2007). Zantedeschia mild mosaic virus, a new widespread virus in calla lily, detected by ELISA, dot-blot hybridization and IC-RT-PCR. Plant Pathol 56, 183-189.
    • (2007) Plant Pathol , vol.56 , pp. 183-189
    • Huang, C.-H.1    Hu, W.-C.2    Yang, T.-C.3    Chang, Y.-C.4
  • 29
    • 0035118223 scopus 로고    scopus 로고
    • Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth
    • Jack, R. L., Sargent, F., Berks, B. C., Sawers, G. & Palmer, T. (2001). Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth. J Bacteriol 183, 1801-1804.
    • (2001) J Bacteriol , vol.183 , pp. 1801-1804
    • Jack, R.L.1    Sargent, F.2    Berks, B.C.3    Sawers, G.4    Palmer, T.5
  • 31
    • 33947366478 scopus 로고    scopus 로고
    • Oxygen reactivity of both respiratory oxidases in Campylobacter jejuni: The cydAB genes encode a cyanide-resistant, low-affinity oxidase that is not of the cytochrome bd type
    • Jackson, R. J., Elvers, K. T., Lee, L. J., Gidley, M. D., Wainwright, L. M., Lightfoot, J., Park, S. F. & Poole, R. K. (2007). Oxygen reactivity of both respiratory oxidases in Campylobacter jejuni: the cydAB genes encode a cyanide-resistant, low-affinity oxidase that is not of the cytochrome bd type. J Bacteriol 189, 1604-1615.
    • (2007) J Bacteriol , vol.189 , pp. 1604-1615
    • Jackson, R.J.1    Elvers, K.T.2    Lee, L.J.3    Gidley, M.D.4    Wainwright, L.M.5    Lightfoot, J.6    Park, S.F.7    Poole, R.K.8
  • 32
    • 58849146951 scopus 로고    scopus 로고
    • Campylobacter in the food supply
    • In, 3rd edn,. Edited by I. Nachamkin, C.M. Szymanski & M.J. Blaser. Washington, DC: American Society for Microbiology
    • Jacobs-Reitsma, W., Lyths, U. & Wagenaar, J. (2008). Campylobacter in the food supply. In Campylobacter, 3rd edn, pp. 627-644. Edited by I. Nachamkin, C. M. Szymanski & M. J. Blaser. Washington, DC: American Society for Microbiology.
    • (2008) Campylobacter , pp. 627-644
    • Jacobs-Reitsma, W.1    Lyths, U.2    Wagenaar, J.3
  • 33
    • 60649087951 scopus 로고    scopus 로고
    • Production, characterization and determination of the real catalytic properties of the putative 'succinate dehydrogenase' from Wolinella succinogenes
    • Juhnke, H. D., Hiltscher, H., Nasiri, H. R., Schwalbe, H. & Lancaster, C. R. (2009). Production, characterization and determination of the real catalytic properties of the putative 'succinate dehydrogenase' from Wolinella succinogenes. Mol Microbiol 71, 1088-1101.
    • (2009) Mol Microbiol , vol.71 , pp. 1088-1101
    • Juhnke, H.D.1    Hiltscher, H.2    Nasiri, H.R.3    Schwalbe, H.4    Lancaster, C.R.5
  • 34
    • 45149092933 scopus 로고    scopus 로고
    • Complexity and versatility in the physiology and metabolism of Campylobacter jejuni
    • In, 3rd edn,. Edited by I. Nachamkin, C.M. Szymanski & M.J. Blaser. Washington, DC: American Society for Microbiology
    • Kelly, D. J. (2008). Complexity and versatility in the physiology and metabolism of Campylobacter jejuni. In Campylobacter, 3rd edn, pp. 41-61. Edited by I. Nachamkin, C. M. Szymanski & M. J. Blaser. Washington, DC: American Society for Microbiology.
    • (2008) Campylobacter , pp. 41-61
    • Kelly, D.J.1
  • 35
    • 84898059539 scopus 로고    scopus 로고
    • Hemerythrins in the microaerophilic bacterium Campylobacter jejuni help protect key iron-sulphur cluster enzymes from oxidative damage
    • Kendall, J. J., Barrero-Tobon, A. M., Hendrixson, D. R. & Kelly, D. J. (2014). Hemerythrins in the microaerophilic bacterium Campylobacter jejuni help protect key iron-sulphur cluster enzymes from oxidative damage. Environ Microbiol 16, 1105-1121.
    • (2014) Environ Microbiol , vol.16 , pp. 1105-1121
    • Kendall, J.J.1    Barrero-Tobon, A.M.2    Hendrixson, D.R.3    Kelly, D.J.4
  • 36
    • 84860354294 scopus 로고    scopus 로고
    • Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells
    • Koch, S., Fritsch, M. J., Buchanan, G. & Palmer, T. (2012). Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells. J Biol Chem 287, 14420-14431.
    • (2012) J Biol Chem , vol.287 , pp. 14420-14431
    • Koch, S.1    Fritsch, M.J.2    Buchanan, G.3    Palmer, T.4
  • 37
    • 77955655119 scopus 로고    scopus 로고
    • Malfolded recombinant Tat substrates are Tatindependently degraded in Escherichia coli
    • Lindenstrauss, U., Matos, C. F., Graubner, W., Robinson, C. & Brüser, T. (2010). Malfolded recombinant Tat substrates are Tatindependently degraded in Escherichia coli. FEBS Lett 584, 3644-3648.
    • (2010) FEBS Lett , vol.584 , pp. 3644-3648
    • Lindenstrauss, U.1    Matos, C.F.2    Graubner, W.3    Robinson, C.4    Brüser, T.5
  • 38
    • 84875618987 scopus 로고    scopus 로고
    • Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria
    • Liu, Y.-W., Denkmann, K., Kosciow, K., Dahl, C. & Kelly, D. J. (2013). Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria. Mol Microbiol 88, 173-188.
    • (2013) Mol Microbiol , vol.88 , pp. 173-188
    • Liu, Y.-W.1    Denkmann, K.2    Kosciow, K.3    Dahl, C.4    Kelly, D.J.5
  • 40
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A., Haas, S. M., Bieber, L. L. & Tolbert, N. E. (1978). A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 87, 206-210.
    • (1978) Anal Biochem , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 41
    • 78650100351 scopus 로고    scopus 로고
    • TatB functions as an oligomeric binding site for folded Tat precursor proteins
    • Maurer, C., Panahandeh, S., Jungkamp, A. C., Moser, M. & Müller, M. (2010). TatB functions as an oligomeric binding site for folded Tat precursor proteins. Mol Biol Cell 21, 4151-4161.
    • (2010) Mol Biol Cell , vol.21 , pp. 4151-4161
    • Maurer, C.1    Panahandeh, S.2    Jungkamp, A.C.3    Moser, M.4    Müller, M.5
  • 42
    • 13444259982 scopus 로고    scopus 로고
    • A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni
    • Myers, J. D. & Kelly, D. J. (2005). A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni. Microbiology 151, 233-242.
    • (2005) Microbiology , vol.151 , pp. 233-242
    • Myers, J.D.1    Kelly, D.J.2
  • 43
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik, I. J., Ladner, C. L. & Turner, R. J. (2001). Identification of a twin-arginine leader-binding protein. Mol Microbiol 40, 323-331.
    • (2001) Mol Microbiol , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 44
    • 41049099591 scopus 로고    scopus 로고
    • A temperature-regulated Campylobacter jejuni gluconate dehydrogenase is involved in respiration-dependent energy conservation and chicken colonization
    • Pajaniappan, M., Hall, J. E., Cawthraw, S. A., Newell, D. G., Gaynor, E. C., Fields, J. A., Rathbun, K. M., Agee, W. A., Burns, C. M. & other authors (2008). A temperature-regulated Campylobacter jejuni gluconate dehydrogenase is involved in respiration-dependent energy conservation and chicken colonization. Mol Microbiol 68, 474-491.
    • (2008) Mol Microbiol , vol.68 , pp. 474-491
    • Pajaniappan, M.1    Hall, J.E.2    Cawthraw, S.A.3    Newell, D.G.4    Gaynor, E.C.5    Fields, J.A.6    Rathbun, K.M.7    Agee, W.A.8    Burns, C.M.9
  • 45
    • 84902267629 scopus 로고    scopus 로고
    • Protein transport by the bacterial Tat pathway
    • Patel, R., Smith, S. M. & Robinson, C. (2014). Protein transport by the bacterial Tat pathway. Biochim Biophys Acta 1843, 1620-1628.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 1620-1628
    • Patel, R.1    Smith, S.M.2    Robinson, C.3
  • 46
    • 33846036912 scopus 로고    scopus 로고
    • Growth of Campylobacter jejuni on nitrate and nitrite: Electron transport to NapA and NrfA via NrfH and distinct roles for NrfA and the globin Cgb in protection against nitrosative stress
    • Pittman, M. S., Elvers, K. T., Lee, L., Jones, M. A., Poole, R. K., Park, S. F. & Kelly, D. J. (2007). Growth of Campylobacter jejuni on nitrate and nitrite: electron transport to NapA and NrfA via NrfH and distinct roles for NrfA and the globin Cgb in protection against nitrosative stress. Mol Microbiol 63, 575-590.
    • (2007) Mol Microbiol , vol.63 , pp. 575-590
    • Pittman, M.S.1    Elvers, K.T.2    Lee, L.3    Jones, M.A.4    Poole, R.K.5    Park, S.F.6    Kelly, D.J.7
  • 48
    • 0033571287 scopus 로고    scopus 로고
    • Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12
    • Potter, L. C. & Cole, J. A. (1999). Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12. Biochem J 344, 69-76.
    • (1999) Biochem J , vol.344 , pp. 69-76
    • Potter, L.C.1    Cole, J.A.2
  • 49
    • 70350116668 scopus 로고    scopus 로고
    • Functional characterization of the twin-arginine translocation system in Campylobacter jejuni
    • Rajashekara, G., Drozd, M., Gangaiah, D., Jeon, B., Liu, Z. & Zhang, Q. (2009). Functional characterization of the twin-arginine translocation system in Campylobacter jejuni. Foodborne Pathog Dis 6, 935-945.
    • (2009) Foodborne Pathog Dis , vol.6 , pp. 935-945
    • Rajashekara, G.1    Drozd, M.2    Gangaiah, D.3    Jeon, B.4    Liu, Z.5    Zhang, Q.6
  • 50
    • 0033532176 scopus 로고    scopus 로고
    • Cotranslocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway
    • Rodrigue, A., Chanal, A., Beck, K., Müller, M. & Wu, L. F. (1999). Cotranslocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway. J Biol Chem 274, 13223-13228.
    • (1999) J Biol Chem , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Müller, M.4    Wu, L.F.5
  • 52
    • 0036038940 scopus 로고    scopus 로고
    • Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway
    • Rose, R. W., Brüser, T., Kissinger, J. C. & Pohlschröder, M. (2002). Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Mol Microbiol 45, 943-950.
    • (2002) Mol Microbiol , vol.45 , pp. 943-950
    • Rose, R.W.1    Brüser, T.2    Kissinger, J.C.3    Pohlschröder, M.4
  • 54
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., Bogsch, E. G., Stanley, N. R., Wexler, M., Robinson, C., Berks, B. C. & Palmer, T. (1998). Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J 17, 3640-3650.
    • (1998) EMBO J , vol.17 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 55
    • 0033579428 scopus 로고    scopus 로고
    • Secindependent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein
    • Sargent, F., Stanley, N. R., Berks, B. C. & Palmer, T. (1999). Secindependent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein. J Biol Chem 274, 36073-36082.
    • (1999) J Biol Chem , vol.274 , pp. 36073-36082
    • Sargent, F.1    Stanley, N.R.2    Berks, B.C.3    Palmer, T.4
  • 56
    • 0036066808 scopus 로고    scopus 로고
    • Growth of Campylobacter jejuni supported by respiration of fumarate, nitrate, nitrite, trimethylamine-N-oxide, or dimethyl sulfoxide requires oxygen
    • Sellars, M. J., Hall, S. J. & Kelly, D. J. (2002). Growth of Campylobacter jejuni supported by respiration of fumarate, nitrate, nitrite, trimethylamine-N-oxide, or dimethyl sulfoxide requires oxygen. J Bacteriol 184, 4187-4196.
    • (2002) J Bacteriol , vol.184 , pp. 4187-4196
    • Sellars, M.J.1    Hall, S.J.2    Kelly, D.J.3
  • 57
    • 70350406435 scopus 로고    scopus 로고
    • A role for tungsten in the biology of Campylobacter jejuni: Tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter
    • Smart, J. P., Cliff, M. J. & Kelly, D. J. (2009). A role for tungsten in the biology of Campylobacter jejuni: tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter. Mol Microbiol 74, 742-757.
    • (2009) Mol Microbiol , vol.74 , pp. 742-757
    • Smart, J.P.1    Cliff, M.J.2    Kelly, D.J.3
  • 58
    • 84878464404 scopus 로고    scopus 로고
    • Nutrient acquisition and metabolism by Campylobacter jejuni
    • Stahl, M., Butcher, J. & Stintzi, A. (2012). Nutrient acquisition and metabolism by Campylobacter jejuni. Front Cell Infect Microbiol 2, 5.
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 5
    • Stahl, M.1    Butcher, J.2    Stintzi, A.3
  • 59
    • 0035190866 scopus 로고    scopus 로고
    • Escherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope
    • Stanley, N. R., Findlay, K., Berks, B. C. & Palmer, T. (2001). Escherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope. J Bacteriol 183, 139-144.
    • (2001) J Bacteriol , vol.183 , pp. 139-144
    • Stanley, N.R.1    Findlay, K.2    Berks, B.C.3    Palmer, T.4
  • 61
    • 78650800583 scopus 로고    scopus 로고
    • Two respiratory enzyme systems in Campylobacter jejuni NCTC 11168 contribute to growth on L-lactate
    • Thomas, M. T., Shepherd, M., Poole, R. K., van Vliet, A. H. M., Kelly, D. J. & Pearson, B. M. (2011). Two respiratory enzyme systems in Campylobacter jejuni NCTC 11168 contribute to growth on L-lactate. Environ Microbiol 13, 48-61.
    • (2011) Environ Microbiol , vol.13 , pp. 48-61
    • Thomas, M.T.1    Shepherd, M.2    Poole, R.K.3    van Vliet, A.H.M.4    Kelly, D.J.5    Pearson, B.M.6
  • 62
    • 3142550604 scopus 로고    scopus 로고
    • Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)
    • Turner, R. J., Papish, A. L. & Sargent, F. (2004). Sequence analysis of bacterial redox enzyme maturation proteins (REMPs). Can J Microbiol 50, 225-238.
    • (2004) Can J Microbiol , vol.50 , pp. 225-238
    • Turner, R.J.1    Papish, A.L.2    Sargent, F.3
  • 63
    • 39749139562 scopus 로고    scopus 로고
    • Functional analysis of a Campylobacter jejuni alkaline phosphatase secreted via the Tat export machinery
    • van Mourik, A., Bleumink-Pluym, N. M., van Dijk, L., van Putten, J. P. & Wösten, M. M. (2008). Functional analysis of a Campylobacter jejuni alkaline phosphatase secreted via the Tat export machinery. Microbiology 154, 584-592.
    • (2008) Microbiology , vol.154 , pp. 584-592
    • van Mourik, A.1    Bleumink-Pluym, N.M.2    van Dijk, L.3    van Putten, J.P.4    Wösten, M.M.5
  • 64
    • 0031690670 scopus 로고    scopus 로고
    • Ironresponsive gene regulation in a Campylobacter jejuni fur mutant
    • van Vliet, A. H. M., Wooldridge, K. G. & Ketley, J. M. (1998). Ironresponsive gene regulation in a Campylobacter jejuni fur mutant. J Bacteriol 180, 5291-5298.
    • (1998) J Bacteriol , vol.180 , pp. 5291-5298
    • van Vliet, A.H.M.1    Wooldridge, K.G.2    Ketley, J.M.3
  • 65
    • 0036126078 scopus 로고    scopus 로고
    • Analysis of gluconeogenic and anaplerotic enzymes in Campylobacter jejuni: An essential role for phosphoenolpyruvate carboxykinase
    • Velayudhan, J. & Kelly, D. J. (2002). Analysis of gluconeogenic and anaplerotic enzymes in Campylobacter jejuni: an essential role for phosphoenolpyruvate carboxykinase. Microbiology 148, 685-694.
    • (2002) Microbiology , vol.148 , pp. 685-694
    • Velayudhan, J.1    Kelly, D.J.2
  • 66
    • 55949099255 scopus 로고    scopus 로고
    • Poultry colonisation with Campylobacter and its control at the primary production level
    • In, 3rd edn,. Edited by I. Nachamkin, C.M. Szymanski & M.J. Blaser. Washington, DC: American Society for Microbiology
    • Wagenaar, J. A., Jacobs-Reitsma, W., Hofshagen, M. & Newell, D. (2008). Poultry colonisation with Campylobacter and its control at the primary production level. In Campylobacter, 3rd edn, pp. 667-678. Edited by I. Nachamkin, C. M. Szymanski & M. J. Blaser. Washington, DC: American Society for Microbiology.
    • (2008) Campylobacter , pp. 667-678
    • Wagenaar, J.A.1    Jacobs-Reitsma, W.2    Hofshagen, M.3    Newell, D.4
  • 67
    • 67349169333 scopus 로고    scopus 로고
    • The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology
    • Weerakoon, D. R., Borden, N. J., Goodson, C. M., Grimes, J. & Olson, J. W. (2009). The role of respiratory donor enzymes in Campylobacter jejuni host colonization and physiology. Microb Pathog 47, 8-15.
    • (2009) Microb Pathog , vol.47 , pp. 8-15
    • Weerakoon, D.R.1    Borden, N.J.2    Goodson, C.M.3    Grimes, J.4    Olson, J.W.5
  • 68
    • 40549083689 scopus 로고    scopus 로고
    • Role of Campylobacter jejuni respiratory oxidases and reductases in host colonization
    • Weingarten, R. A., Grimes, J. L. & Olson, J. W. (2008). Role of Campylobacter jejuni respiratory oxidases and reductases in host colonization. Appl Environ Microbiol 74, 1367-1375.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1367-1375
    • Weingarten, R.A.1    Grimes, J.L.2    Olson, J.W.3
  • 69
    • 67749101854 scopus 로고    scopus 로고
    • The dualfunctioning fumarate reductase is the sole succinate: Quinone reductase in Campylobacter jejuni and is required for full host colonization
    • Weingarten, R. A., Taveirne, M. E. & Olson, J. W. (2009). The dualfunctioning fumarate reductase is the sole succinate: quinone reductase in Campylobacter jejuni and is required for full host colonization. J Bacteriol 191, 5293-5300.
    • (2009) J Bacteriol , vol.191 , pp. 5293-5300
    • Weingarten, R.A.1    Taveirne, M.E.2    Olson, J.W.3
  • 70
    • 0034595796 scopus 로고    scopus 로고
    • TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export
    • Wexler, M., Sargent, F., Jack, R. L., Stanley, N. R., Bogsch, E. G., Robinson, C., Berks, B. C. & Palmer, T. (2000). TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export. J Biol Chem 275, 16717-16722.
    • (2000) J Biol Chem , vol.275 , pp. 16717-16722
    • Wexler, M.1    Sargent, F.2    Jack, R.L.3    Stanley, N.R.4    Bogsch, E.G.5    Robinson, C.6    Berks, B.C.7    Palmer, T.8
  • 71
    • 0031718841 scopus 로고    scopus 로고
    • A modified overlap extension PCR method to create chimeric genes in the absence of restriction enzymes
    • Wurch, T., Lestienne, F. & Pauwels, P. J. (1998). A modified overlap extension PCR method to create chimeric genes in the absence of restriction enzymes. Biotechnol Tech 12, 653-657.
    • (1998) Biotechnol Tech , vol.12 , pp. 653-657
    • Wurch, T.1    Lestienne, F.2    Pauwels, P.J.3
  • 72
    • 0035873543 scopus 로고    scopus 로고
    • Functional reconstitution of bacterial Tat translocation in vitro
    • Yahr, T. L. & Wickner, W. T. (2001). Functional reconstitution of bacterial Tat translocation in vitro. EMBO J 20, 2472-2479.
    • (2001) EMBO J , vol.20 , pp. 2472-2479
    • Yahr, T.L.1    Wickner, W.T.2
  • 73
    • 15744391209 scopus 로고    scopus 로고
    • A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway
    • Zhang, J. W., Butland, G., Greenblatt, J. F., Emili, A. & Zamble, D. B. (2005). A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway. J Biol Chem 280, 4360-4366.
    • (2005) J Biol Chem , vol.280 , pp. 4360-4366
    • Zhang, J.W.1    Butland, G.2    Greenblatt, J.F.3    Emili, A.4    Zamble, D.B.5


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