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Volumn 187, Issue 8, 2005, Pages 2920-2925

Positive selection for loss-of-function tat mutations identifies critical residues required for TatA activity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHLORAMPHENICOL ACETYLTRANSFERASE; PROTEIN TATA; UNCLASSIFIED DRUG;

EID: 14644444922     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.8.2920-2925.2005     Document Type: Article
Times cited : (32)

References (34)
  • 1
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alanii, M., I. Luke, S. Deitermann, G. Eisner, H. G. Koch, J. Brunner, J., and M. Muller. 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
    • Alanii, M.1    Luke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.G.5    Brunner, J.J.6    Muller, M.7
  • 2
    • 0041656271 scopus 로고    scopus 로고
    • Energy use by biological protein transport pathways
    • Alder, N. N., and S. M. Theg. 2003. Energy use by biological protein transport pathways. Trends Biochem. Sci. 28:442-451.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 442-451
    • Alder, N.N.1    Theg, S.M.2
  • 3
    • 0037468404 scopus 로고    scopus 로고
    • Identification of key regions within the Escherichia coli TatAB subunits
    • Barrett, C. M. L., J. E. Mathers, and C. Robinson. 2003. Identification of key regions within the Escherichia coli TatAB subunits. FEBS Lett. 537:42-46.
    • (2003) FEBS Lett. , vol.537 , pp. 42-46
    • Barrett, C.M.L.1    Mathers, J.E.2    Robinson, C.3
  • 4
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolomé, B., Y. Jubete, E. Martínez, and F. de la Cruz. 1991. Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102:75-78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolomé, B.1    Jubete, Y.2    Martínez, E.3    De La Cruz, F.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
    • 0141672034 scopus 로고    scopus 로고
    • The Tat protein translocation pathway and its role in microbial physiology
    • Berks, B. C., T. Palmer, and F. Sargent. 2003. The Tat protein translocation pathway and its role in microbial physiology. Adv. Microb. Physiol. 47:187-254.
    • (2003) Adv. Microb. Physiol. , vol.47 , pp. 187-254
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 7
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch, E., 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 plastids and mitochondria. J. Biol. Chem. 273: 18003-18006.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18003-18006
    • Bogsch, E.1    Sargent, F.2    Stanley, N.R.3    Berks, B.C.4    Robinson, C.5    Palmer, T.6
  • 8
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis, A., J. E. Mathers, J. D. Thomas, C. M. Barrett, and C. Robinson. 2001. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 276:20213-20219.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20213-20219
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.M.4    Robinson, C.5
  • 9
    • 0036274596 scopus 로고    scopus 로고
    • Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
    • Buchanan, G., E. de Leeuw, N. R. Stanley, M. Wexler, B. C. Berks, F. Sargent, and T. Palmer. 2002. Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis. Mol. Microbiol. 43:1457-1470.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1457-1470
    • Buchanan, G.1    De Leeuw, E.2    Stanley, N.R.3    Wexler, M.4    Berks, B.C.5    Sargent, F.6    Palmer, T.7
  • 10
    • 0000366608 scopus 로고
    • Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: In vivo probe for transcriptional control sequences
    • Casadaban, M. J., and S. N. Cohen. 1979. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences. Proc. Natl. Acad. Sci. USA 76:4530-4533.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4530-4533
    • Casadaban, M.J.1    Cohen, S.N.2
  • 11
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • Cline, K., and H. Mori. 2001. Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J. Cell Biol. 154:719-729.
    • (2001) J. Cell Biol. , vol.154 , pp. 719-729
    • Cline, K.1    Mori, H.2
  • 12
    • 0034049316 scopus 로고    scopus 로고
    • Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies
    • Daugherty, P. S., G. Chen, B. L. Iverson, and G. Georgiou. 2000. Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies. Proc. Natl. Acad. Sci. USA 97:2029-2034.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2029-2034
    • Daugherty, P.S.1    Chen, G.2    Iverson, B.L.3    Georgiou, G.4
  • 13
    • 0035812905 scopus 로고    scopus 로고
    • Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
    • De Leeuw, E., I. Porcelli, F. Sargent, T. Palmer, and B. C. Berks. 2001. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett. 506:143-148.
    • (2001) FEBS Lett. , vol.506 , pp. 143-148
    • De Leeuw, E.1    Porcelli, I.2    Sargent, F.3    Palmer, T.4    Berks, B.C.5
  • 14
    • 0037119435 scopus 로고    scopus 로고
    • Genetic analysis of the twin arginine translocator secretion pathway in bacteria
    • De Lisa, 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
    • De Lisa, M.P.1    Samuelson, P.2    Palmer, T.3    Georgiou, G.4
  • 15
    • 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., E. de Leeuw, I. Porcelli, G. Buchanan, B. C. Berks, and T. Palmer. 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
  • 17
    • 0036431451 scopus 로고    scopus 로고
    • In vivo assessment of the Tat signal peptide specificity in Escherichia coli
    • Ize, B., F. Gérard, and L.-F. Wu. 2002. In vivo assessment of the Tat signal peptide specificity in Escherichia coli. Arch. Microbiol. 178:548-553.
    • (2002) Arch. Microbiol. , vol.178 , pp. 548-553
    • Ize, B.1    Gérard, F.2    Wu, L.-F.3
  • 18
    • 0038460119 scopus 로고    scopus 로고
    • Role of the Escherichia coli Tat pathway in outer membrane integrity
    • Ize, B., N. R. Stanley, G. Buchanan, and T. Palmer. 2003. Role of the Escherichia coli Tat pathway in outer membrane integrity. Mol. Microbiol. 48:1183-1193.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1183-1193
    • Ize, B.1    Stanley, N.R.2    Buchanan, G.3    Palmer, T.4
  • 19
    • 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., F. Sargent, B. C. Berks, G. Sawers, and T. Palmer. 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
  • 21
    • 0036837744 scopus 로고    scopus 로고
    • Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation
    • Lee, P. A., G. Buchanan, N. R. Stanley, B. C. Berks, and T. Palmer. 2002. Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation. J. Bacteriol. 184:5871-5879.
    • (2002) J. Bacteriol. , vol.184 , pp. 5871-5879
    • Lee, P.A.1    Buchanan, G.2    Stanley, N.R.3    Berks, B.C.4    Palmer, T.5
  • 22
    • 0037092039 scopus 로고    scopus 로고
    • A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
    • Mori, J., and K. Cline. 2002. A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase. J. Cell Biol. 157:205-210.
    • (2002) J. Cell Biol. , vol.157 , pp. 205-210
    • Mori, J.1    Cline, K.2
  • 25
    • 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
  • 26
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., E. 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.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 27
    • 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. 274:36073-36083.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36073-36083
    • Sargent, F.1    Stanley, N.R.2    Berks, B.C.3    Palmer, T.4
  • 28
    • 0034832014 scopus 로고    scopus 로고
    • Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
    • Sargent, F., U. Gohlke, E. de Leeuw, N. R. Stanley, T. Palmer, H. R. Saibil, and B. C. Berks. 2001. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur. J. Biochem. 268:3361-3367.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3361-3367
    • Sargent, F.1    Gohlke, U.2    De Leeuw, E.3    Stanley, N.R.4    Palmer, T.5    Saibil, H.R.6    Berks, B.C.7
  • 29
    • 0023948847 scopus 로고
    • The inducible trimethylamine-N-oxide reductase of Escherichia coli K12: Biochemical and immunological studies
    • Silvestro, A., J. Pommier, and G. Giordano. 1988. The inducible trimethylamine-N-oxide reductase of Escherichia coli K12: biochemical and immunological studies. Biochim. Biophys. Acta 954:1-13.
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 1-13
    • Silvestro, A.1    Pommier, J.2    Giordano, G.3
  • 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. 257:11591-11596.
    • (2000) J. Biol. Chem. , vol.257 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 32
    • 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
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 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


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