메뉴 건너뛰기




Volumn 190, Issue 19, 2008, Pages 6428-6438

Identification of functional Tat signal sequences in Mycobacterium tuberculosis proteins

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL PROTEIN; BETA LACTAMASE; DIPEPTIDE; PHOSPHOLIPASE C; VIRULENCE FACTOR;

EID: 52649121849     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00749-08     Document Type: Article
Times cited : (68)

References (64)
  • 1
    • 0345621667 scopus 로고    scopus 로고
    • Bange, F. C., F. M. Collins, and W. R. Jacobs, Jr. 1999. Survival of mice infected with Mycobacterium smegmatis containing large DNA fragments from Mycobacterium tuberculosis. Tuber. Lung Dis. 79:171-180.
    • Bange, F. C., F. M. Collins, and W. R. Jacobs, Jr. 1999. Survival of mice infected with Mycobacterium smegmatis containing large DNA fragments from Mycobacterium tuberculosis. Tuber. Lung Dis. 79:171-180.
  • 2
    • 0026761861 scopus 로고
    • Rapid mycobacterial plasmid analysis by electroduction between Mycobacterium spp. and Escherichia coli
    • Baulard, A., C. Jourdan, A. Mercenier, and C. Locht. 1992. Rapid mycobacterial plasmid analysis by electroduction between Mycobacterium spp. and Escherichia coli. Nucleic Acids Res. 20:4105.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4105
    • Baulard, A.1    Jourdan, C.2    Mercenier, A.3    Locht, C.4
  • 5
    • 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
  • 6
    • 0036436740 scopus 로고    scopus 로고
    • Genetic methods for deciphering virulence determinants of Mycobacterium tuberculosis
    • Braunstein, M., S. S. Bardarov, and W. R. J. Jacobs. 2002. Genetic methods for deciphering virulence determinants of Mycobacterium tuberculosis. Methods Enzymol. 358:67-99.
    • (2002) Methods Enzymol , vol.358 , pp. 67-99
    • Braunstein, M.1    Bardarov, S.S.2    Jacobs, W.R.J.3
  • 7
    • 0035212925 scopus 로고    scopus 로고
    • Braunstein, M., A. M. Brown, S. Kurtz, and W. R. Jacobs, Jr. 2001. Two nonredundant SecA homologues function in mycobacteria. J. Bacteriol. 183:6979-6990.
    • Braunstein, M., A. M. Brown, S. Kurtz, and W. R. Jacobs, Jr. 2001. Two nonredundant SecA homologues function in mycobacteria. J. Bacteriol. 183:6979-6990.
  • 8
    • 9644266608 scopus 로고    scopus 로고
    • Dissecting the twin-arginine translocation pathway using genome-wide analysis
    • Bronstein, P., M. Marrichi, and M. P. DeLisa. 2004. Dissecting the twin-arginine translocation pathway using genome-wide analysis. Res. Microbiol. 155:803-810.
    • (2004) Res. Microbiol , vol.155 , pp. 803-810
    • Bronstein, P.1    Marrichi, M.2    DeLisa, M.P.3
  • 9
    • 28844461575 scopus 로고    scopus 로고
    • Identification of a twin-arginine translocation system in Pseudomonas syringae pv. tomato DC3000 and its contribution to pathogenicity and fitness
    • Bronstein, P. A., M. Marrichi, S. Cartinhour, D. J. Schneider, and M. P. DeLisa. 2005. Identification of a twin-arginine translocation system in Pseudomonas syringae pv. tomato DC3000 and its contribution to pathogenicity and fitness. J. Bacteriol. 187:8450-8461.
    • (2005) J. Bacteriol , vol.187 , pp. 8450-8461
    • Bronstein, P.A.1    Marrichi, M.2    Cartinhour, S.3    Schneider, D.J.4    DeLisa, M.P.5
  • 10
    • 31644447233 scopus 로고    scopus 로고
    • The Tat pathway of the plant pathogen Pseudomonas syringae is required for optimal virulence
    • Caldelari, I., S. Mann, C. Crooks, and T. Palmer. 2006. The Tat pathway of the plant pathogen Pseudomonas syringae is required for optimal virulence. Mol. Plant-Microbe Interact. 19:200-212.
    • (2006) Mol. Plant-Microbe Interact , vol.19 , pp. 200-212
    • Caldelari, I.1    Mann, S.2    Crooks, C.3    Palmer, T.4
  • 11
    • 0036774642 scopus 로고    scopus 로고
    • Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv
    • Camus, J. C., M. J. Pryor, C. Medigue, and S. T. Cole. 2002. Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv. Microbiology 148:2967-2973.
    • (2002) Microbiology , vol.148 , pp. 2967-2973
    • Camus, J.C.1    Pryor, M.J.2    Medigue, C.3    Cole, S.T.4
  • 12
    • 0030951308 scopus 로고    scopus 로고
    • PlcR1 and PlcR2 are putative calcium-binding proteins required for secretion of the hemolytic phospholipase C of Pseudomonas aeruginosa
    • Cota-Gomez, A., A. I. Vasil, J. Kadurugamuwa, T. J. Beveridge, H. P. Schweizer, and M. L. Vasil. 1997. PlcR1 and PlcR2 are putative calcium-binding proteins required for secretion of the hemolytic phospholipase C of Pseudomonas aeruginosa. Infect. Immun. 65:2904-2913.
    • (1997) Infect. Immun , vol.65 , pp. 2904-2913
    • Cota-Gomez, A.1    Vasil, A.I.2    Kadurugamuwa, J.3    Beveridge, T.J.4    Schweizer, H.P.5    Vasil, M.L.6
  • 13
    • 0040537042 scopus 로고    scopus 로고
    • Competition between Sec- and TAT-dependent protein translocation in Escherichia coli
    • Cristobal, S., J. W. de Gier, H. Nielsen, and G. von Heijne. 1999. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18:2982-2990.
    • (1999) EMBO J , vol.18 , pp. 2982-2990
    • Cristobal, S.1    de Gier, J.W.2    Nielsen, H.3    von Heijne, G.4
  • 14
    • 0037119435 scopus 로고    scopus 로고
    • Genetic analysis of the twin arginine translocator secretion pathway in bacteria
    • DeLisa, M. P., P. Samuelson, T. Palmer, and G. Georgiou. 2002. Genetic analysis of the twin arginine translocator secretion pathway in bacteria. J. Biol. Chem. 277:29825-29831.
    • (2002) J. Biol. Chem , vol.277 , pp. 29825-29831
    • DeLisa, M.P.1    Samuelson, P.2    Palmer, T.3    Georgiou, G.4
  • 15
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa, M. P., D. Tullman, and G. Georgiou. 2003. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. USA 100:6115-6120.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 16
    • 0037317124 scopus 로고    scopus 로고
    • Prokaryotic utilization of the twin-arginine translocation pathway: A genomic survey
    • Dilks, K., R. W. Rose, E. Hartmann, and M. Pohlschroder. 2003. Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey. J. Bacteriol. 185:1478-1483.
    • (2003) J. Bacteriol , vol.185 , pp. 1478-1483
    • Dilks, K.1    Rose, R.W.2    Hartmann, E.3    Pohlschroder, M.4
  • 17
    • 0037307748 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens twin-arginine-dependent translocation is important for virulence, flagellation, and chemotaxis but not type IV secretion
    • Ding, Z., and P. J. Christie. 2003. Agrobacterium tumefaciens twin-arginine-dependent translocation is important for virulence, flagellation, and chemotaxis but not type IV secretion. J. Bacteriol. 185:760-771.
    • (2003) J. Bacteriol , vol.185 , pp. 760-771
    • Ding, Z.1    Christie, P.J.2
  • 18
    • 14044262957 scopus 로고    scopus 로고
    • Flores, A. R., L. M. Parsons, and M. S. Pavelka, Jr. 2005. Genetic analysis of the beta-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to beta-lactam antibiotics. Microbiology 151:521-532.
    • Flores, A. R., L. M. Parsons, and M. S. Pavelka, Jr. 2005. Genetic analysis of the beta-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to beta-lactam antibiotics. Microbiology 151:521-532.
  • 19
    • 34447505050 scopus 로고    scopus 로고
    • Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway
    • Gibbons, H. S., F. Wolschendorf, M. Abshire, M. Niederweis, and M. Braunstein. 2007. Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway. J. Bacteriol. 189:5090-5100.
    • (2007) J. Bacteriol , vol.189 , pp. 5090-5100
    • Gibbons, H.S.1    Wolschendorf, F.2    Abshire, M.3    Niederweis, M.4    Braunstein, M.5
  • 20
    • 36549088956 scopus 로고    scopus 로고
    • Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins
    • Gimenez, M. I., K. Dilks, and M. Pohlschroder. 2007. Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins. Mol. Microbiol. 66:1597-1606.
    • (2007) Mol. Microbiol , vol.66 , pp. 1597-1606
    • Gimenez, M.I.1    Dilks, K.2    Pohlschroder, M.3
  • 21
    • 0033634971 scopus 로고    scopus 로고
    • Glickman, M. S., J. S. Cox, and W. R. Jacobs, Jr. 2000. A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis. Mol. Cell 5:717-727.
    • Glickman, M. S., J. S. Cox, and W. R. Jacobs, Jr. 2000. A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis. Mol. Cell 5:717-727.
  • 22
    • 0034059725 scopus 로고    scopus 로고
    • Identification of secreted proteins of Mycobacterium tuberculosis by a bioinformatic approach
    • Gomez, M., S. Johnson, and M. L. Gennaro. 2000. Identification of secreted proteins of Mycobacterium tuberculosis by a bioinformatic approach. Infect. Immun. 68:2323-2327.
    • (2000) Infect. Immun , vol.68 , pp. 2323-2327
    • Gomez, M.1    Johnson, S.2    Gennaro, M.L.3
  • 23
    • 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., A. Schierhorn, and T. Bruser. 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    Bruser, T.3
  • 24
    • 11144329901 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain
    • Gu, S., J. Chen, K. M. Dobos, E. M. Bradbury, J. T. Belisle, and X. Chen. 2003. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell. Proteomics 2:1284-1296.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1284-1296
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4    Belisle, J.T.5    Chen, X.6
  • 25
    • 0033565687 scopus 로고    scopus 로고
    • The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding
    • Halbig, D., T. Wiegert, N. Blaudeck, R. Freudl, and G. A. Sprenger. 1999. The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding. Eur. J. Biochem. 263:543-551.
    • (1999) Eur. J. Biochem , vol.263 , pp. 543-551
    • Halbig, D.1    Wiegert, T.2    Blaudeck, N.3    Freudl, R.4    Sprenger, G.A.5
  • 26
    • 0035907063 scopus 로고    scopus 로고
    • A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif
    • Hinsley, A. P., N. R. Stanley, T. Palmer, and B. C. Berks. 2001. A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif. FEBS Lett. 497:45-49.
    • (2001) FEBS Lett , vol.497 , pp. 45-49
    • Hinsley, A.P.1    Stanley, N.R.2    Palmer, T.3    Berks, B.C.4
  • 27
    • 0036088769 scopus 로고    scopus 로고
    • Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery
    • Ignatova, Z., C. Hornle, A. Nurk, and V. Kasche. 2002. Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery. Biochem. Biophys. Res. Commun. 291:146-149.
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 146-149
    • Ignatova, Z.1    Hornle, C.2    Nurk, A.3    Kasche, V.4
  • 29
    • 0030036237 scopus 로고    scopus 로고
    • Biochemical and molecular analysis of phospholipase C and phospholipase D activity in mycobacteria
    • Johansen, K. A., R. E. Gill, and M. L. Vasil. 1996. Biochemical and molecular analysis of phospholipase C and phospholipase D activity in mycobacteria. Infect. Immun. 64:3259-3266.
    • (1996) Infect. Immun , vol.64 , pp. 3259-3266
    • Johansen, K.A.1    Gill, R.E.2    Vasil, M.L.3
  • 30
    • 33644782616 scopus 로고    scopus 로고
    • The twin arginine translocation system is essential for virulence of Yersinia pseudotuberculosis
    • Lavander, M., S. K. Ericsson, J. E. Broms, and A. Forsberg. 2006. The twin arginine translocation system is essential for virulence of Yersinia pseudotuberculosis. Infect. Immun. 74:1768-1776.
    • (2006) Infect. Immun , vol.74 , pp. 1768-1776
    • Lavander, M.1    Ericsson, S.K.2    Broms, J.E.3    Forsberg, A.4
  • 31
  • 32
    • 34249701192 scopus 로고    scopus 로고
    • Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv
    • Malen, H., F. S. Berven, K. E. Fladmark, and H. G. Wiker. 2007. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics 7:1702-1718.
    • (2007) Proteomics , vol.7 , pp. 1702-1718
    • Malen, H.1    Berven, F.S.2    Fladmark, K.E.3    Wiker, H.G.4
  • 33
    • 35448941836 scopus 로고    scopus 로고
    • Beta-lactamase can function as a reporter of bacterial protein export during Mycobacterium tuberculosis infection of host cells
    • McCann, J. R., J. A. McDonough, M. S. Pavelka, and M. Braunstein. 2007. Beta-lactamase can function as a reporter of bacterial protein export during Mycobacterium tuberculosis infection of host cells. Microbiology 153:3350-3359.
    • (2007) Microbiology , vol.153 , pp. 3350-3359
    • McCann, J.R.1    McDonough, J.A.2    Pavelka, M.S.3    Braunstein, M.4
  • 34
    • 27744493918 scopus 로고    scopus 로고
    • The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases
    • McDonough, J. A., K. E. Hacker, A. R. Flores, M. S. Pavelka, Jr., and M. Braunstein. 2005. The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases. J. Bacteriol. 187:7667-7679.
    • (2005) J. Bacteriol , vol.187 , pp. 7667-7679
    • McDonough, J.A.1    Hacker, K.E.2    Flores, A.R.3    Pavelka Jr., M.S.4    Braunstein, M.5
  • 35
    • 0035477117 scopus 로고    scopus 로고
    • The Sec protein-translocation pathway
    • Mori, H., and K. Ito. 2001. The Sec protein-translocation pathway. Trends Microbiol. 9:494-500.
    • (2001) Trends Microbiol , vol.9 , pp. 494-500
    • Mori, H.1    Ito, K.2
  • 36
    • 0037062507 scopus 로고    scopus 로고
    • Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis
    • Ochsner, U. A., A. Snyder, A. I. Vasil, and M. L. Vasil. 2002. Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis. Proc. Natl. Acad. Sci. USA 99:8312-8317.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8312-8317
    • Ochsner, U.A.1    Snyder, A.2    Vasil, A.I.3    Vasil, M.L.4
  • 37
    • 0019413905 scopus 로고    scopus 로고
    • Oliver, D. B., and J. Beckwith. 1981. E. coli mutant pleiotropically defective in the export of secreted proteins. Cell 25:765-772.
    • Oliver, D. B., and J. Beckwith. 1981. E. coli mutant pleiotropically defective in the export of secreted proteins. Cell 25:765-772.
  • 38
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik, I. J., C. L. Ladner, and R. J. Turner. 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
  • 39
    • 16244380460 scopus 로고    scopus 로고
    • Export of complex cofactor-containing proteins by the bacterial Tat pathway
    • Palmer, T., F. Sargent, and B. C. Berks. 2005. Export of complex cofactor-containing proteins by the bacterial Tat pathway. Trends Microbiol. 13:175-180.
    • (2005) Trends Microbiol , vol.13 , pp. 175-180
    • Palmer, T.1    Sargent, F.2    Berks, B.C.3
  • 40
    • 33847396185 scopus 로고    scopus 로고
    • An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway
    • Perez-Rodriguez, R., A. C. Fisher, J. D. Perlmutter, M. G. Hicks, A. Chanal, C. L. Santini, L. F. Wu, T. Palmer, and M. P. Delisa. 2007. An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway. J. Mol. Biol. 367:715-730.
    • (2007) J. Mol. Biol , vol.367 , pp. 715-730
    • Perez-Rodriguez, R.1    Fisher, A.C.2    Perlmutter, J.D.3    Hicks, M.G.4    Chanal, A.5    Santini, C.L.6    Wu, L.F.7    Palmer, T.8    Delisa, M.P.9
  • 41
    • 32444443415 scopus 로고    scopus 로고
    • Characterization of the twin-arginine translocase secretion system of Mycobacterium smegmatis
    • Posey, J. E., T. M. Shinnick, and F. D. Quinn. 2006. Characterization of the twin-arginine translocase secretion system of Mycobacterium smegmatis. J. Bacteriol. 188:1332-1340.
    • (2006) J. Bacteriol , vol.188 , pp. 1332-1340
    • Posey, J.E.1    Shinnick, T.M.2    Quinn, F.D.3
  • 42
    • 0042825530 scopus 로고    scopus 로고
    • Contribution of the twin arginine translocation system to the virulence of enterohemorrhagic Escherichia coli O157:H7
    • Pradel, N., C. Ye, V. Livrelli, J. Xu, B. Joly, and L. F. Wu. 2003. Contribution of the twin arginine translocation system to the virulence of enterohemorrhagic Escherichia coli O157:H7. Infect. Immun. 71:4908-4916.
    • (2003) Infect. Immun , vol.71 , pp. 4908-4916
    • Pradel, N.1    Ye, C.2    Livrelli, V.3    Xu, J.4    Joly, B.5    Wu, L.F.6
  • 45
    • 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., T. Bruser, J. C. Kissinger, and M. Pohlschroder. 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    Bruser, T.2    Kissinger, J.C.3    Pohlschroder, M.4
  • 46
    • 16244414601 scopus 로고    scopus 로고
    • The Legionella pneumophila tatB gene facilitates secretion of phospholipase C, growth under iron-limiting conditions, and intracellular infection
    • Rossier, O., and N. P. Cianciotto. 2005. The Legionella pneumophila tatB gene facilitates secretion of phospholipase C, growth under iron-limiting conditions, and intracellular infection. Infect. Immun. 73:2020-2032.
    • (2005) Infect. Immun , vol.73 , pp. 2020-2032
    • Rossier, O.1    Cianciotto, N.P.2
  • 47
    • 33748765246 scopus 로고    scopus 로고
    • Inactivation of Rv2525c, a substrate of the twin arginine translocation (Tat) system of Mycobacterium tuberculosis, increases β-lactam susceptibility and virulence
    • Saint-Joanis, B., C. Demangel, M. Jackson, P. Brodin, L. Marsollier, H. Boshoff, and S. T. Cole. 2006. Inactivation of Rv2525c, a substrate of the twin arginine translocation (Tat) system of Mycobacterium tuberculosis, increases β-lactam susceptibility and virulence. J. Bacteriol. 188:6669-6679.
    • (2006) J. Bacteriol , vol.188 , pp. 6669-6679
    • Saint-Joanis, B.1    Demangel, C.2    Jackson, M.3    Brodin, P.4    Marsollier, L.5    Boshoff, H.6    Cole, S.T.7
  • 49
    • 0035896573 scopus 로고    scopus 로고
    • Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock
    • Santini, C. L., A. Bernadac, M. Zhang, A. Chanal, B. Ize, C. Blanco, and L. F. Wu. 2001. Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J. Biol. Chem. 276:8159-8164.
    • (2001) J. Biol. Chem , vol.276 , pp. 8159-8164
    • Santini, C.L.1    Bernadac, A.2    Zhang, M.3    Chanal, A.4    Ize, B.5    Blanco, C.6    Wu, L.F.7
  • 50
    • 0035940515 scopus 로고    scopus 로고
    • Comprehensive identification of conditionally essential genes in mycobacteria
    • Sassetti, C. M., D. H. Boyd, and E. J. Rubin. 2001. Comprehensive identification of conditionally essential genes in mycobacteria. Proc. Natl. Acad. Sci. USA 98:12712-12717.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12712-12717
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 51
    • 2542574741 scopus 로고    scopus 로고
    • Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology
    • Schmidt, F., S. Donahoe, K. Hagens, J. Mattow, U. E. Schaible, S. H. Kaufmann, R. Aebersold, and P. R. Jungblut. 2004. Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology. Mol. Cell. Proteomics 3:24-42.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 24-42
    • Schmidt, F.1    Donahoe, S.2    Hagens, K.3    Mattow, J.4    Schaible, U.E.5    Kaufmann, S.H.6    Aebersold, R.7    Jungblut, P.R.8
  • 53
    • 0025081151 scopus 로고    scopus 로고
    • Snapper, S. B., R. E. Melton, S. Mustafa, T. Kieser, and W. R. Jacobs, Jr. 1990. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4:1911-1919.
    • Snapper, S. B., R. E. Melton, S. Mustafa, T. Kieser, and W. R. Jacobs, Jr. 1990. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4:1911-1919.
  • 54
    • 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., T. Palmer, and B. C. Berks. 2000. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275:11591-11596.
    • (2000) J. Biol. Chem , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 56
    • 7944226058 scopus 로고    scopus 로고
    • Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components
    • Sutcliffe, I. C., and D. J. Harrington. 2004. Lipoproteins of Mycobacterium tuberculosis: an abundant and functionally diverse class of cell envelope components. FEMS Microbiol. Rev. 28:645-659.
    • (2004) FEMS Microbiol. Rev , vol.28 , pp. 645-659
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 57
    • 0035181362 scopus 로고    scopus 로고
    • Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli
    • Thomas, J. D., R. A. Daniel, J. Errington, and C. Robinson. 2001. Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol. Microbiol. 39:47-53.
    • (2001) Mol. Microbiol , vol.39 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 60
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • Voulhoux, R., G. Ball, B. Ize, M. L. Vasil, A. Lazdunski, L. F. Wu, and A. Filloux. 2001. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20:6735-6741.
    • (2001) EMBO J , vol.20 , pp. 6735-6741
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5    Wu, L.F.6    Filloux, A.7
  • 61
    • 0026578808 scopus 로고
    • Three N-terminal domains of beta-1,3-glucanase A1 are involved in binding to insoluble beta-1,3-glucan
    • Watanabe, T., N. Kasahara, K. Aida, and H. Tanaka. 1992. Three N-terminal domains of beta-1,3-glucanase A1 are involved in binding to insoluble beta-1,3-glucan. J. Bacteriol. 174:186-190.
    • (1992) J. Bacteriol , vol.174 , pp. 186-190
    • Watanabe, T.1    Kasahara, N.2    Aida, K.3    Tanaka, H.4
  • 62
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • Wickner, W., and R. Schekman. 2005. Protein translocation across biological membranes. Science 310:1452-1456.
    • (2005) Science , vol.310 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 63
    • 37349115561 scopus 로고    scopus 로고
    • A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life
    • Widdick, D. A., R. T. Eijlander, J. M. van Dijl, O. P. Kuipers, and T. Palmer. 2008. A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life. J. Mol. Biol. 375:595-603.
    • (2008) J. Mol. Biol , vol.375 , pp. 595-603
    • Widdick, D.A.1    Eijlander, R.T.2    van Dijl, J.M.3    Kuipers, O.P.4    Palmer, T.5
  • 64
    • 52649148244 scopus 로고    scopus 로고
    • posting date. WHO information tuberculosis fact sheet
    • World Health Organization. 2007, posting date. WHO information tuberculosis fact sheet. http://www.who.int/mediacentre/factsheets/fs104/en/.
    • (2007)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.