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Volumn 374, Issue 2, 2007, Pages 283-291

Escherichia coli tatC Mutations that Suppress Defective Twin-Arginine Transporter Signal Peptides

Author keywords

flow cytometry; signal peptide recognition; suppressors; TatC; twin arginine translocase

Indexed keywords

AMINO ACID; ARGININE; DIPEPTIDE; GENE PRODUCT; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LYSINE; OXIDOREDUCTASE; PROTEIN TATB; PROTEIN TATC; SIGNAL PEPTIDE; TRANSACTIVATOR PROTEIN; TRIMETHYLAMINE OXIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 35549001419     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.09.050     Document Type: Article
Times cited : (45)

References (36)
  • 1
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks B.C. A common export pathway for proteins binding complex redox cofactors?. Mol. Microbiol. 22 (1996) 393-404
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 2
    • 0036296099 scopus 로고    scopus 로고
    • In vivo dissection of the Tat translocation pathway in Escherichia coli
    • Ize B., Gerard F., Zhang M., Chanal A., Voulhoux R., Palmer T., et al. In vivo dissection of the Tat translocation pathway in Escherichia coli. J. Mol. Biol. 317 (2002) 327-335
    • (2002) J. Mol. Biol. , vol.317 , pp. 327-335
    • Ize, B.1    Gerard, F.2    Zhang, M.3    Chanal, A.4    Voulhoux, R.5    Palmer, T.6
  • 3
    • 0348150717 scopus 로고    scopus 로고
    • Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis
    • Jongbloed J.D., Antelmann H., Hecker M., Nijland R., Bron S., Airaksinen U., et al. Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis. J. Biol. Chem. 277 (2002) 44068-44078
    • (2002) J. Biol. Chem. , vol.277 , pp. 44068-44078
    • Jongbloed, J.D.1    Antelmann, H.2    Hecker, M.3    Nijland, R.4    Bron, S.5    Airaksinen, U.6
  • 4
    • 0036479116 scopus 로고    scopus 로고
    • The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system
    • Pop O., Martin U., Abel C., and Muller J.P. The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system. J. Biol. Chem. 277 (2002) 3268-3273
    • (2002) J. Biol. Chem. , vol.277 , pp. 3268-3273
    • Pop, O.1    Martin, U.2    Abel, C.3    Muller, J.P.4
  • 5
    • 0036276602 scopus 로고    scopus 로고
    • Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system
    • Yen M.R., Tseng Y.H., Nguyen E.H., Wu L.F., and Saier Jr. M.H. Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system. Arch. Microbiol. 177 (2002) 441-450
    • (2002) Arch. Microbiol. , vol.177 , pp. 441-450
    • Yen, M.R.1    Tseng, Y.H.2    Nguyen, E.H.3    Wu, L.F.4    Saier Jr., M.H.5
  • 6
    • 23044487649 scopus 로고    scopus 로고
    • The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
    • Gohlke U., Pullan L., McDevitt C.A., Porcelli I., de Leeuw E., Palmer T., et al. The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc. Natl. Acad. Sci. USA 102 (2005) 10482-10486
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10482-10486
    • Gohlke, U.1    Pullan, L.2    McDevitt, C.A.3    Porcelli, I.4    de Leeuw, E.5    Palmer, T.6
  • 7
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami M., Luke I., Deitermann S., Eisner G., Koch H.G., Brunner J., and Muller M. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12 (2003) 937-946
    • (2003) Mol. Cell , vol.12 , pp. 937-946
    • Alami, M.1    Luke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.G.5    Brunner, J.6    Muller, M.7
  • 8
    • 34247111382 scopus 로고    scopus 로고
    • The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex
    • Gerard F., and Cline K. The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. J. Biol. Chem. 282 (2007) 5263-5272
    • (2007) J. Biol. Chem. , vol.282 , pp. 5263-5272
    • Gerard, F.1    Cline, K.2
  • 9
    • 33646837543 scopus 로고    scopus 로고
    • Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
    • Dabney-Smith C., Mori H., and Cline K. Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J. Biol. Chem. 281 (2006) 5476-5483
    • (2006) J. Biol. Chem. , vol.281 , pp. 5476-5483
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 10
    • 0036136514 scopus 로고    scopus 로고
    • A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif
    • Buchanan G., Sargent F., Berks B.C., and Palmer T. A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif. Arch. Microbiol. 177 (2001) 107-112
    • (2001) Arch. Microbiol. , vol.177 , pp. 107-112
    • Buchanan, G.1    Sargent, F.2    Berks, B.C.3    Palmer, T.4
  • 11
    • 0037119435 scopus 로고    scopus 로고
    • Genetic analysis of the twin arginine translocator secretion pathway in bacteria
    • DeLisa M.P., Samuelson P., Palmer T., and Georgiou G. Genetic analysis of the twin arginine translocator secretion pathway in bacteria. J. Biol. Chem. 277 (2002) 29825-29831
    • (2002) J. Biol. Chem. , vol.277 , pp. 29825-29831
    • DeLisa, M.P.1    Samuelson, P.2    Palmer, T.3    Georgiou, G.4
  • 12
    • 34247239812 scopus 로고    scopus 로고
    • Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities
    • Kreutzenbeck P., Kroger C., Lausberg F., Blaudeck N., Sprenger G.A., and Freudl R. Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities. J. Biol. Chem. 282 (2007) 7903-7911
    • (2007) J. Biol. Chem. , vol.282 , pp. 7903-7911
    • Kreutzenbeck, P.1    Kroger, C.2    Lausberg, F.3    Blaudeck, N.4    Sprenger, G.A.5    Freudl, R.6
  • 13
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko I., Seidel M., Sauer R.T., and Baker T.A. A specificity-enhancing factor for the ClpXP degradation machine. Science 289 (2000) 2354-2356
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 15
    • 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., and Palmer T. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 273 (1998) 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
  • 16
    • 0028816556 scopus 로고
    • Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction
    • Fromant M., Blanquet S., and Plateau P. Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction. Anal. Biochem. 224 (1995) 347-353
    • (1995) Anal. Biochem. , vol.224 , pp. 347-353
    • Fromant, M.1    Blanquet, S.2    Plateau, P.3
  • 17
    • 0036274596 scopus 로고    scopus 로고
    • Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
    • Buchanan G., Leeuw E., Stanley N.R., Wexler M., Berks B.C., Sargent F., and Palmer T. Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis. Mol. Microbiol. 43 (2002) 1457-1470
    • (2002) Mol. Microbiol. , vol.43 , pp. 1457-1470
    • Buchanan, G.1    Leeuw, E.2    Stanley, N.R.3    Wexler, M.4    Berks, B.C.5    Sargent, F.6    Palmer, T.7
  • 18
    • 0036412417 scopus 로고    scopus 로고
    • Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
    • de Leeuw E., Granjon T., Porcelli I., Alami M., Carr S.B., Muller M., et al. Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes. J. Mol. Biol. 322 (2002) 1135-1146
    • (2002) J. Mol. Biol. , vol.322 , pp. 1135-1146
    • de Leeuw, E.1    Granjon, T.2    Porcelli, I.3    Alami, M.4    Carr, S.B.5    Muller, M.6
  • 19
    • 34547631621 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis and topological mapping of the Escherichia coli twin-arginine translocase TatC component
    • Punginelli C., Maldonado B., Grahl S., Jack R., Alami M., Schroder J., et al. Cysteine scanning mutagenesis and topological mapping of the Escherichia coli twin-arginine translocase TatC component. J. Bacteriol. 189 (2007) 5482-5494
    • (2007) J. Bacteriol. , vol.189 , pp. 5482-5494
    • Punginelli, C.1    Maldonado, B.2    Grahl, S.3    Jack, R.4    Alami, M.5    Schroder, J.6
  • 20
    • 0043209015 scopus 로고    scopus 로고
    • Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA
    • Ilbert M., Mejean V., Giudici-Orticoni M.T., Samama J.P., and Iobbi-Nivol C. Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA. J. Biol. Chem. 278 (2003) 28787-28792
    • (2003) J. Biol. Chem. , vol.278 , pp. 28787-28792
    • Ilbert, M.1    Mejean, V.2    Giudici-Orticoni, M.T.3    Samama, J.P.4    Iobbi-Nivol, C.5
  • 21
    • 0032568823 scopus 로고    scopus 로고
    • TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli
    • Pommier J., Mejean V., Giordano G., and Iobbi-Nivol C. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli. J. Biol. Chem. 273 (1998) 16615-16620
    • (1998) J. Biol. Chem. , vol.273 , pp. 16615-16620
    • Pommier, J.1    Mejean, V.2    Giordano, G.3    Iobbi-Nivol, C.4
  • 22
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini C.L., Ize B., Chanal A., Muller M., Giordano G., and Wu L.F. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17 (1998) 101-112
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.L.1    Ize, B.2    Chanal, A.3    Muller, M.4    Giordano, G.5    Wu, L.F.6
  • 23
    • 0035853704 scopus 로고    scopus 로고
    • Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli
    • Gon S., Giudici-Orticoni M.T., Mejean V., and Iobbi-Nivol C. Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. J. Biol. Chem. 276 (2001) 11545-11551
    • (2001) J. Biol. Chem. , vol.276 , pp. 11545-11551
    • Gon, S.1    Giudici-Orticoni, M.T.2    Mejean, V.3    Iobbi-Nivol, C.4
  • 25
    • 0034697156 scopus 로고    scopus 로고
    • The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
    • Stanley N.R., Palmer T., and Berks B.C. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275 (2000) 11591-11596
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 26
    • 0023948847 scopus 로고
    • The inducible trimethylamine-N-oxide reductase of Escherichia coli K12: biochemical and immunological studies
    • Silvestro A., Pommier J., and Giordano G. The inducible trimethylamine-N-oxide reductase of Escherichia coli K12: biochemical and immunological studies. Biochim. Biophys. Acta 954 (1988) 1-13
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 1-13
    • Silvestro, A.1    Pommier, J.2    Giordano, G.3
  • 27
    • 0034945221 scopus 로고    scopus 로고
    • Involvement of N-acetylmuramyl-l-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli
    • Heidrich C., Templin M.F., Ursinus A., Merdanovic M., Berger J., Schwarz H., et al. Involvement of N-acetylmuramyl-l-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli. Mol. Microbiol. 41 (2001) 167-178
    • (2001) Mol. Microbiol. , vol.41 , pp. 167-178
    • Heidrich, C.1    Templin, M.F.2    Ursinus, A.3    Merdanovic, M.4    Berger, J.5    Schwarz, H.6
  • 28
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt T.G., and de Boer P.A. The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol. Microbiol. 48 (2003) 1171-1182
    • (2003) Mol. Microbiol. , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 29
    • 33746649568 scopus 로고    scopus 로고
    • Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli
    • Priyadarshini R., Popham D.L., and Young K.D. Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli. J. Bacteriol. 188 (2006) 5345-5355
    • (2006) J. Bacteriol. , vol.188 , pp. 5345-5355
    • Priyadarshini, R.1    Popham, D.L.2    Young, K.D.3
  • 31
    • 3843140548 scopus 로고    scopus 로고
    • A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis
    • Ki J.J., Kawarasaki Y., Gam J., Harvey B.R., Iverson B.L., and Georgiou G. A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis. J. Mol. Biol. 341 (2004) 901-909
    • (2004) J. Mol. Biol. , vol.341 , pp. 901-909
    • Ki, J.J.1    Kawarasaki, Y.2    Gam, J.3    Harvey, B.R.4    Iverson, B.L.5    Georgiou, G.6
  • 33
    • 0037155803 scopus 로고    scopus 로고
    • Essential cytoplasmic domains in the Escherichia coli TatC protein
    • Allen S.C., Barrett C.M., Ray N., and Robinson C. Essential cytoplasmic domains in the Escherichia coli TatC protein. J. Biol. Chem. 277 (2002) 10362-10366
    • (2002) J. Biol. Chem. , vol.277 , pp. 10362-10366
    • Allen, S.C.1    Barrett, C.M.2    Ray, N.3    Robinson, C.4
  • 34
    • 1642523788 scopus 로고    scopus 로고
    • Dual topology of the Escherichia coli TatA protein
    • Gouffi K., Gerard F., Santini C.L., and Wu L.F. Dual topology of the Escherichia coli TatA protein. J. Biol. Chem. 279 (2004) 11608-11615
    • (2004) J. Biol. Chem. , vol.279 , pp. 11608-11615
    • Gouffi, K.1    Gerard, F.2    Santini, C.L.3    Wu, L.F.4
  • 35
    • 33947243288 scopus 로고    scopus 로고
    • The entire N-terminal half of TatC is involved in twin-arginine precursor binding
    • Holzapfel E., Eisner G., Alami M., Barrett C.M., Buchanan G., Luke I., et al. The entire N-terminal half of TatC is involved in twin-arginine precursor binding. Biochemistry 46 (2007) 2892-2898
    • (2007) Biochemistry , vol.46 , pp. 2892-2898
    • Holzapfel, E.1    Eisner, G.2    Alami, M.3    Barrett, C.M.4    Buchanan, G.5    Luke, I.6
  • 36
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme
    • Sawers R.G., Ballantine S.P., and Boxer D.H. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J. Bacteriol. 164 (1985) 1324-1331
    • (1985) J. Bacteriol. , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3


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