메뉴 건너뛰기




Volumn 185, Issue 4, 2003, Pages 1478-1483

Prokaryotic utilization of the twin-arginine translocation pathway: A genomic survey

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALKALINE PHOSPHATASE; AMINO ACID; ARGININE; PHOSPHOLIPASE C;

EID: 0037317124     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.4.1478-1483.2003     Document Type: Article
Times cited : (208)

References (37)
  • 3
    • 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
  • 4
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastid and mitochondria
    • Bogsch, E. G., F. Sargent, N. R. Stanley, B. C. Berks, C. Robinson, and T. Palmer. 1998. An essential component of a novel bacterial protein export system with homologues in plastid 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
  • 5
    • 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., F. Sargent, B. C. Berks, and T. Palmer. 2001. 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. 177:107-112.
    • (2001) Arch. Microbiol. , vol.177 , pp. 107-112
    • Buchanan, G.1    Sargent, F.2    Berks, B.C.3    Palmer, T.4
  • 6
    • 0029079118 scopus 로고
    • A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase
    • Chaddock, A. M., A. Mant, I. Karnauchov, S. Brink, R. G. Herrmann, R. B. Klosgen, and C. Robinson. 1995. A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase. EMBO J. 14:2715-2722.
    • (1995) EMBO J. , vol.14 , pp. 2715-2722
    • Chaddock, A.M.1    Mant, A.2    Karnauchov, I.3    Brink, S.4    Herrmann, R.G.5    Klosgen, R.B.6    Robinson, C.7
  • 7
    • 0026787702 scopus 로고
    • Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP
    • Cline, K., W. F. Ettinger, and S. M. Theg. 1992. Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J. Biol. Chem. 267:2688-2696.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 8
    • 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
  • 9
    • 0033008601 scopus 로고    scopus 로고
    • Protein targeting to the bacterial cytoplasmic membrane
    • Fekkes, P., and A. J. Driessen. 1999. Protein targeting to the bacterial cytoplasmic membrane. Microbiol. Mol. Biol. Rev. 63:161-173.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 161-173
    • Fekkes, P.1    Driessen, A.J.2
  • 10
    • 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
  • 11
    • 0032567332 scopus 로고    scopus 로고
    • The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane
    • Hynds, P. J., D. Robinson, and C. Robinson. 1998. The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane. J. Biol. Chem. 273:34868-34874.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34868-34874
    • Hynds, P.J.1    Robinson, D.2    Robinson, C.3
  • 12
    • 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
  • 15
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack, K., W. Mothes, and T. Rapoport. 1998. Protein translocation: tunnel vision. Cell 92:381-390.
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.1    Mothes, W.2    Rapoport, T.3
  • 16
    • 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
  • 17
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 18
    • 0026646678 scopus 로고
    • Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a betalactamase fusion protein
    • Niviere, V., S. L. Wong, and G. Voordouw. 1992. Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a betalactamase fusion protein. J. Gen. Microbiol. 138:2173-2183.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2173-2183
    • Niviere, V.1    Wong, S.L.2    Voordouw, G.3
  • 19
    • 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
  • 20
    • 0038415649 scopus 로고    scopus 로고
    • Protein translocation in the three domains of life: Variations on a theme
    • Pohlschroder, M., W. A. Prinz, E. Hartmann, and J. Beckwith. 1997. Protein translocation in the three domains of life: variations on a theme. Cell 91:563-566.
    • (1997) Cell , vol.91 , pp. 563-566
    • Pohlschroder, M.1    Prinz, W.A.2    Hartmann, E.3    Beckwith, J.4
  • 21
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin-arginine translocation pathway
    • Robinson, C., and A. Bolhuis. 2001. Protein targeting by the twin-arginine translocation pathway. Nat. Rev. Mol. Cell Biol. 2:350-356.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 350-356
    • Robinson, C.1    Bolhuis, A.2
  • 22
    • 0033532176 scopus 로고    scopus 로고
    • Cotranslocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway
    • Rodrigue, A., A. Chanal, K. Beck, M. Muller, and L. F. Wu. 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    Muller, M.4    Wu, L.F.5
  • 23
    • 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
  • 24
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini, C. L., B. Ize, A. Chanal, M. Muller, G. Giordano, and L. F. Wu. 1998. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:101-112.
    • (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
  • 25
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., E. G. Bogsch, N. R. Stanley, M. Wexler, C. Robinson, B. C. Berks, and T. Palmer. 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
  • 26
    • 0033579428 scopus 로고    scopus 로고
    • Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein
    • Sargent, F., N. R. Stanley, B. C. Berks, and T. Palmer. 1999. Sec-independent 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
  • 29
    • 0035190866 scopus 로고    scopus 로고
    • Escherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope
    • Stanley, N. R., K. Findlay, B. C. Berks, and T. Palmer. 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
  • 30
    • 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
  • 31
    • 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
  • 32
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker, R., and A. Barkan. 1995. Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J. 14:3905-3914.
    • (1995) EMBO J. , vol.14 , pp. 3905-3914
    • Voelker, R.1    Barkan, A.2
  • 33
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne, G. 1990. The signal peptide. J. Membr. Biol. 115:195-201.
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 34
    • 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
  • 35
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • Weiner, J. H., P. T. Bilous, G. M. Shaw, S. P. Lubitz, L. Frost, G. H. Thomas, J. A. Cole, and R. J. Turner. 1998. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93:93-101.
    • (1998) Cell , vol.93 , pp. 93-101
    • Weiner, J.H.1    Bilous, P.T.2    Shaw, G.M.3    Lubitz, S.P.4    Frost, L.5    Thomas, G.H.6    Cole, J.A.7    Turner, R.J.8
  • 36
    • 0033996321 scopus 로고    scopus 로고
    • Bacterial twin-arginine signal peptide-dependent protein translocation pathway: Evolution and mechanism
    • Wu, L. F., B. Ize, A. Chanal, Y. Quentin, and G. Fichant. 2000. Bacterial twin-arginine signal peptide-dependent protein translocation pathway: evolution and mechanism. J. Mol. Microbiol. Biotechnol. 2:179-189.
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 179-189
    • Wu, L.F.1    Ize, B.2    Chanal, A.3    Quentin, Y.4    Fichant, G.5
  • 37
    • 0036276602 scopus 로고    scopus 로고
    • Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system
    • Yen, M. R., Y. H. Tseng, E. H. Nguyen, L. F. Wu, and M. H. Saier, Jr. 2002. Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system. Arch. Microbiol. 177:441-450.
    • (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 M.H., Jr.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.