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Volumn 20, Issue 10, 2001, Pages 2472-2479

Functional reconstitution of bacterial Tat translocation in vitro

Author keywords

Membrane proteins; Tat translocase; TatABCE

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CARRIER PROTEIN; SIGNAL PEPTIDE; TRANSACTIVATOR PROTEIN;

EID: 0035873543     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.10.2472     Document Type: Article
Times cited : (142)

References (33)
  • 1
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-Derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolome, B., Jubete, Y., Martinez, E. and de la Cruz, F. (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
    • Bartolome, B.1    Jubete, Y.2    Martinez, E.3    De La Cruz, F.4
  • 2
    • 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
  • 5
    • 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. (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
  • 6
    • 0034697250 scopus 로고    scopus 로고
    • Subunit interactions in the twin-arginine translocase complex of Escherichia coli
    • Bolhuis, A., Bogsch, E.G. and Robinson, C. (2000) Subunit interactions in the twin-arginine translocase complex of Escherichia coli. FEBS Lett., 472, 88-92.
    • (2000) FEBS Lett. , vol.472 , pp. 88-92
    • Bolhuis, A.1    Bogsch, E.G.2    Robinson, C.3
  • 7
    • 0028985671 scopus 로고
    • The ΔpH-driven, ATP-independent protein translocation machanism in the chloroplast thylakoid membrane. Kinetics and energetics
    • Brock, I.W., Mills, J.D., Robinson, D. and Robinson, C. (1995) The ΔpH-driven, ATP-independent protein translocation machanism in the chloroplast thylakoid membrane. Kinetics and energetics. J. Biol. Chem., 270, 1657-1662.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1657-1662
    • Brock, I.W.1    Mills, J.D.2    Robinson, D.3    Robinson, C.4
  • 8
    • 0025087853 scopus 로고
    • The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation
    • Brundage, L., Hendrick, J.P., Schiebel, E., Driessen, A.J.M. and Wickner, W. (1990) The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell, 62, 649-657.
    • (1990) Cell , vol.62 , pp. 649-657
    • Brundage, L.1    Hendrick, J.P.2    Schiebel, E.3    Driessen, A.J.M.4    Wickner, W.5
  • 9
    • 0026768696 scopus 로고
    • SecY, SecE and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase
    • Brundage, L., Fimmel, C.J., Mizushima, S. and Wickner, W. (1992) SecY, SecE and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase. J. Biol. Chem., 267, 4166-4170.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4166-4170
    • Brundage, L.1    Fimmel, C.J.2    Mizushima, S.3    Wickner, W.4
  • 10
    • 0000366608 scopus 로고
    • Lactose genes fused to exogenous promoters in one step using Mud-lac bacteriophage: In vivo probe for transcriptional control sequences
    • Casadaban, M.J. and Cohen, S.N. (1979) Lactose genes fused to exogenous promoters in one step using Mud-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
    • 0031792216 scopus 로고    scopus 로고
    • Potential receptor function of three homologous components, TatA, TatB, and TatE, of the twin-arginine signal sequence-dependent metalloenzyme translocation pathway in Escherichia coli
    • Chanal, A., Santini, C.-L. and Wu, L.-F. (1998) Potential receptor function of three homologous components, TatA, TatB, and TatE, of the twin-arginine signal sequence-dependent metalloenzyme translocation pathway in Escherichia coli. Mol. Microbiol., 30, 673-678.
    • (1998) Mol. Microbiol. , vol.30 , pp. 673-678
    • Chanal, A.1    Santini, C.-L.2    Wu, L.-F.3
  • 12
    • 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., Ettinger, W.F. and Theg, S.M. (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
  • 13
    • 0028945041 scopus 로고
    • A monomeric, tightly folded stromal intermediate on the ΔpH-dependent thylakoidal protein transport pathway
    • Creighton, A.M., Hulford, A., Mant, A., Robinson, D. and Robinson, C. (1995) A monomeric, tightly folded stromal intermediate on the ΔpH-dependent thylakoidal protein transport pathway. J. Biol. Chem., 270, 1663-1669.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1663-1669
    • Creighton, A.M.1    Hulford, A.2    Mant, A.3    Robinson, D.4    Robinson, C.5
  • 14
    • 0040537042 scopus 로고    scopus 로고
    • Competition between Sec-and Tat-dependent protein translocation in Escherichia coli
    • Cristobal, S., de Gier, J.-W., Nielsen, H. and von Heijne, G. (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
  • 15
    • 0032971998 scopus 로고    scopus 로고
    • Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane
    • Dalbey, R.E. and Robinson, C. (1999) Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane. Trends Biochem. Sci., 24, 17-22
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 17-22
    • Dalbey, R.E.1    Robinson, C.2
  • 16
    • 0029148784 scopus 로고
    • SecYEG and SecA are the stoichiometric components of preprotein translocase
    • Douville, K., Price, A., Eichler, J., Economou, A. and Wickner, W. (1995) SecYEG and SecA are the stoichiometric components of preprotein translocase. J. Biol. Chem., 270, 20106-20111.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20106-20111
    • Douville, K.1    Price, A.2    Eichler, J.3    Economou, A.4    Wickner, W.5
  • 17
    • 0030745847 scopus 로고    scopus 로고
    • Distinct catalytic roles of the SecYE, SecG, and SecDFyajC subunits of preprotein translocase
    • Duong, F. and Wickner, W.T. (1997) Distinct catalytic roles of the SecYE, SecG, and SecDFyajC subunits of preprotein translocase. EMBO J., 16, 4871-4879.
    • (1997) EMBO J. , vol.16 , pp. 4871-4879
    • Duong, F.1    Wickner, W.T.2
  • 19
    • 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., Robinson, D. and Robinson, C. (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
  • 20
    • 0025781325 scopus 로고
    • A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane
    • Mould, R.M. and Robinson, C. (1991) A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J. Biol. Chem., 266, 12189-12193.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12189-12193
    • Mould, R.M.1    Robinson, C.2
  • 21
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor
    • Paetzel, M., Dalbey, R.E. and Strynadka, N.C. (1998) Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor. Nature, 396, 186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 22
    • 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., Muller, M. and 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    Muller, M.4    Wu, L.-F.5
  • 23
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic protein translocation system in Escherichia coli
    • Santini, C.-L., Ize, B., Chanal, A., Muller, M., Giordano, G. and Wu, L.-F. (1998) A novel Sec-independent periplasmic protein translocation system 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
  • 24
    • 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. and 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
  • 25
    • 0033579428 scopus 로고    scopus 로고
    • Sec-independent protein translocation in Escherichia coli
    • Sargent, F., Stanley, N.R., Berks, B.C. and Palmer, T. (1999) Sec-independent protein translocation in Escherichia coli. 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
  • 26
    • 0030722626 scopus 로고    scopus 로고
    • Sec-independent protein translocation by the maize Hcf106 protein
    • Settles, A., Yonetani, A., Baron, A., Bush, D., Cline, K. and Martienssen, R. (1997) Sec-independent protein translocation by the maize Hcf106 protein. Science, 278, 1467-1470.
    • (1997) Science , vol.278 , pp. 1467-1470
    • Settles, A.1    Yonetani, A.2    Baron, A.3    Bush, D.4    Cline, K.5    Martienssen, R.6
  • 27
    • 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. (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
  • 28
    • 0032539535 scopus 로고    scopus 로고
    • Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation
    • Teter, S.A. and Theg, S.M. (1998) Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation. Proc. Natl Acad. Sci. USA, 95, 1590-1594.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1590-1594
    • Teter, S.A.1    Theg, S.M.2
  • 29
    • 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., Daniel, R.A., Errington, J. and Robinson, C. (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
  • 30
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker, R. and Barkan, A. (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
  • 31
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • Weiner, J.H., Bilous, P.T., Shaw, G.M., Lubitz, S.P., Frost, L., Thomas, G.H., Cole, J.A. and Turner, R.J. (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
  • 32
    • 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. and 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
  • 33
    • 0029914812 scopus 로고    scopus 로고
    • Genetic relationship between the 53-and 49-kilodalton forms of exoenzyme S from Pseudomonas aeruginosa
    • Yahr, T.L., Barbieri, J.T. and Frank, D.W. (1996) Genetic relationship between the 53-and 49-kilodalton forms of exoenzyme S from Pseudomonas aeruginosa. J. Bacteriol., 178, 1412-1419.
    • (1996) J. Bacteriol. , vol.178 , pp. 1412-1419
    • Yahr, T.L.1    Barbieri, J.T.2    Frank, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.