메뉴 건너뛰기




Volumn 27, Issue 1, 2014, Pages 32-37

Structural biology of tat protein transport

Author keywords

[No Author keywords available]

Indexed keywords

TATA PROTEIN; TATC PROTEIN; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG; CYTOPLASM PROTEIN; MEMBRANE PROTEIN; PROTEIN TATA; PROTEIN TATC; SIGNAL PEPTIDE;

EID: 84897492556     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.03.003     Document Type: Review
Times cited : (21)

References (37)
  • 1
    • 84862501228 scopus 로고    scopus 로고
    • The twin-arginine translocation (Tat) protein export pathway
    • Palmer T., Berks B.C. The twin-arginine translocation (Tat) protein export pathway. Nat Rev Microbiol 2012, 10:483-496.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 483-496
    • Palmer, T.1    Berks, B.C.2
  • 2
    • 84879888089 scopus 로고    scopus 로고
    • Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways
    • Kudva R., Denks K., Kuhn P., Vogt A., Muller M., Koch H.G. Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways. Res Microbiol 2013, 164:505-534.
    • (2013) Res Microbiol , vol.164 , pp. 505-534
    • Kudva, R.1    Denks, K.2    Kuhn, P.3    Vogt, A.4    Muller, M.5    Koch, H.G.6
  • 3
    • 84871734172 scopus 로고    scopus 로고
    • Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition
    • Celedon J.M., Cline K. Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition. Biochim Biophys Acta 2013, 1833:341-351.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 341-351
    • Celedon, J.M.1    Cline, K.2
  • 4
    • 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 1996, 22:393-404.
    • (1996) Mol Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 5
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • Cline K., Mori H. Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J Cell Biol 2001, 154:719-729.
    • (2001) J Cell Biol , vol.154 , pp. 719-729
    • Cline, K.1    Mori, H.2
  • 6
    • 0037092039 scopus 로고    scopus 로고
    • A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase
    • Mori H., Cline K. A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase. J Cell Biol 2002, 157:205-210.
    • (2002) J Cell Biol , vol.157 , pp. 205-210
    • Mori, H.1    Cline, K.2
  • 7
    • 33646837543 scopus 로고    scopus 로고
    • Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
    • Dabney-Smith C., Mori H., Cline K. Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J Biol Chem 2006, 281:5476-5483.
    • (2006) J Biol Chem , vol.281 , pp. 5476-5483
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 8
    • 84884317508 scopus 로고    scopus 로고
    • Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system
    • Alcock F., Baker M.A., Greene N.P., Palmer T., Wallace M.I., Berks B.C. Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system. Proc Natl Acad Sci U S A 2013, 110:E3650-E3659.
    • (2013) Proc Natl Acad Sci U S A , vol.110
    • Alcock, F.1    Baker, M.A.2    Greene, N.P.3    Palmer, T.4    Wallace, M.I.5    Berks, B.C.6
  • 9
    • 84880969972 scopus 로고    scopus 로고
    • Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells
    • Rose P., Frobel J., Graumann P.L., Muller M. Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells. PLoS ONE 2013, 8:e69488.
    • (2013) PLoS ONE , vol.8
    • Rose, P.1    Frobel, J.2    Graumann, P.L.3    Muller, M.4
  • 10
    • 84873267127 scopus 로고    scopus 로고
    • Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts
    • Pal D., Fite K., Dabney-Smith C. Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts. Plant Physiol 2013, 161:990-1001.
    • (2013) Plant Physiol , vol.161 , pp. 990-1001
    • Pal, D.1    Fite, K.2    Dabney-Smith, C.3
  • 12
    • 84877583210 scopus 로고    scopus 로고
    • The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation
    • Ramasamy S., Abrol R., Suloway C.J., Clemons W.M. The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation. Structure 2013, 21:777-788.
    • (2013) Structure , vol.21 , pp. 777-788
    • Ramasamy, S.1    Abrol, R.2    Suloway, C.J.3    Clemons, W.M.4
  • 13
    • 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., Palmer T. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem 1998, 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
  • 15
    • 84859736979 scopus 로고    scopus 로고
    • Mapping precursor-binding site on TatC subunit of twin arginine-specific protein translocase by site-specific photo cross-linking
    • Zoufaly S., Frobel J., Rose P., Flecken T., Maurer C., Moser M., Muller M. Mapping precursor-binding site on TatC subunit of twin arginine-specific protein translocase by site-specific photo cross-linking. J Biol Chem 2012, 287:13430-13441.
    • (2012) J Biol Chem , vol.287 , pp. 13430-13441
    • Zoufaly, S.1    Frobel, J.2    Rose, P.3    Flecken, T.4    Maurer, C.5    Moser, M.6    Muller, M.7
  • 16
    • 84862746985 scopus 로고    scopus 로고
    • Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli
    • Lausberg F., Fleckenstein S., Kreutzenbeck P., Frobel J., Rose P., Muller M., Freudl R. Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli. PLoS ONE 2012, 7:e39867.
    • (2012) PLoS ONE , vol.7
    • Lausberg, F.1    Fleckenstein, S.2    Kreutzenbeck, P.3    Frobel, J.4    Rose, P.5    Muller, M.6    Freudl, R.7
  • 17
    • 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., Freudl R. Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities. J Biol Chem 2007, 282:7903-7911.
    • (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
  • 18
    • 35549001419 scopus 로고    scopus 로고
    • Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides
    • Strauch E.M., Georgiou G. Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides. J Mol Biol 2007, 374:283-291.
    • (2007) J Mol Biol , vol.374 , pp. 283-291
    • Strauch, E.M.1    Georgiou, G.2
  • 19
    • 84876773076 scopus 로고    scopus 로고
    • Mapping the signal peptide binding and oligomer contact sites of the core subunit of the pea twin arginine protein translocase
    • Ma X., Cline K. Mapping the signal peptide binding and oligomer contact sites of the core subunit of the pea twin arginine protein translocase. Plant Cell 2013, 25:999-1015.
    • (2013) Plant Cell , vol.25 , pp. 999-1015
    • Ma, X.1    Cline, K.2
  • 20
    • 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., Cline K. The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. J Biol Chem 2007, 282:5263-5272.
    • (2007) J Biol Chem , vol.282 , pp. 5263-5272
    • Gerard, F.1    Cline, K.2
  • 21
    • 84871785408 scopus 로고    scopus 로고
    • Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB
    • Frobel J., Rose P., Lausberg F., Blummel A.S., Freudl R., Muller M. Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB. Nat Commun 2012, 3:1311.
    • (2012) Nat Commun , vol.3 , pp. 1311
    • Frobel, J.1    Rose, P.2    Lausberg, F.3    Blummel, A.S.4    Freudl, R.5    Muller, M.6
  • 22
    • 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., Muller M. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol Cell 2003, 12:937-946.
    • (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
  • 23
    • 33646596629 scopus 로고    scopus 로고
    • Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site
    • Gerard F., Cline K. Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site. J Biol Chem 2006, 281:6130-6135.
    • (2006) J Biol Chem , vol.281 , pp. 6130-6135
    • Gerard, F.1    Cline, K.2
  • 24
    • 78449239236 scopus 로고    scopus 로고
    • Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis
    • Hu Y., Zhao E., Li H., Xia B., Jin C. Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis. J Am Chem Soc 2010, 132:15942-15944.
    • (2010) J Am Chem Soc , vol.132 , pp. 15942-15944
    • Hu, Y.1    Zhao, E.2    Li, H.3    Xia, B.4    Jin, C.5
  • 26
    • 78449242888 scopus 로고    scopus 로고
    • Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy
    • Walther T.H., Grage S.L., Roth N., Ulrich A.S. Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy. J Am Chem Soc 2010, 132:15945-15956.
    • (2010) J Am Chem Soc , vol.132 , pp. 15945-15956
    • Walther, T.H.1    Grage, S.L.2    Roth, N.3    Ulrich, A.S.4
  • 27
    • 84860354294 scopus 로고    scopus 로고
    • Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells
    • Koch S., Fritsch M.J., Buchanan G., Palmer T. Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells. J Biol Chem 2012, 287:14420-14431.
    • (2012) J Biol Chem , vol.287 , pp. 14420-14431
    • Koch, S.1    Fritsch, M.J.2    Buchanan, G.3    Palmer, T.4
  • 28
    • 34548208263 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis and disulfide mapping studies of the TatA component of the bacterial twin arginine translocase
    • Greene N.P., Porcelli I., Buchanan G., Hicks M.G., Schermann S.M., Palmer T., Berks B.C. Cysteine scanning mutagenesis and disulfide mapping studies of the TatA component of the bacterial twin arginine translocase. J Biol Chem 2007, 282:23937-23945.
    • (2007) J Biol Chem , vol.282 , pp. 23937-23945
    • Greene, N.P.1    Porcelli, I.2    Buchanan, G.3    Hicks, M.G.4    Schermann, S.M.5    Palmer, T.6    Berks, B.C.7
  • 29
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis A., Mathers J.E., Thomas J.D., Barrett C.M., Robinson C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J Biol Chem 2001, 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
  • 31
    • 0036274596 scopus 로고    scopus 로고
    • Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
    • Buchanan G., de Leeuw E., Stanley N.R., Wexler M., Berks B.C., Sargent F., Palmer T. Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis. Mol Microbiol 2002, 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
  • 32
    • 79959551982 scopus 로고    scopus 로고
    • Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase
    • Maldonado B., Buchanan G., Muller M., Berks B.C., Palmer T. Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase. J Mol Microbiol Biotechnol 2011, 20:168-175.
    • (2011) J Mol Microbiol Biotechnol , vol.20 , pp. 168-175
    • Maldonado, B.1    Buchanan, G.2    Muller, M.3    Berks, B.C.4    Palmer, T.5
  • 34
    • 77951978000 scopus 로고    scopus 로고
    • Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported
    • Ma X., Cline K. Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported. EMBO J 2010, 29:1477-1488.
    • (2010) EMBO J , vol.29 , pp. 1477-1488
    • Ma, X.1    Cline, K.2
  • 35
    • 84885381858 scopus 로고    scopus 로고
    • Signal peptide etiquette during assembly of a complex respiratory enzyme
    • James M.J., Coulthurst S.J., Palmer T., Sargent F. Signal peptide etiquette during assembly of a complex respiratory enzyme. Mol Microbiol 2013, 90:400-414.
    • (2013) Mol Microbiol , vol.90 , pp. 400-414
    • James, M.J.1    Coulthurst, S.J.2    Palmer, T.3    Sargent, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.