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Volumn 1833, Issue 8, 2013, Pages 1811-1819

Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores

Author keywords

Electron microscopy; Gram positive bacteria; Protein transport; Single particle image processing; Tat translocation

Indexed keywords

TATA BINDING PROTEIN;

EID: 84877830628     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.03.028     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 84862501228 scopus 로고    scopus 로고
    • The twin-arginine translocation (Tat) protein export pathway. Nature reviews
    • Palmer T., Berks B.C. The twin-arginine translocation (Tat) protein export pathway. Nature reviews. Microbiology 2012, 10:483-496.
    • (2012) Microbiology , vol.10 , pp. 483-496
    • Palmer, T.1    Berks, B.C.2
  • 3
    • 18844442890 scopus 로고    scopus 로고
    • The Tat pathway in bacteria and chloroplasts (review)
    • Müller M., Klösgen R.B. The Tat pathway in bacteria and chloroplasts (review). Mol. Membr. Biol. 2005, 22:113-121.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 113-121
    • Müller, M.1    Klösgen, R.B.2
  • 4
    • 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., Theg S.M. 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. 1992, 267:2688-2696.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 6
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini C.-L., Ize B., Chanal A., Müller M., Giordano G., Wu L.-F. A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 1998, 17:101-112.
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.-L.1    Ize, B.2    Chanal, A.3    Müller, M.4    Giordano, G.5    Wu, L.-F.6
  • 7
    • 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., Mant A., Karnauchov I., Brink S., Herrmann R.G., Klösgen R.B., Robinson C. 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. 1995, 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    Klösgen, R.B.6    Robinson, C.7
  • 8
    • 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., Berks B.C. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 2000, 275:11591-11596.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 9
    • 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., Palmer T. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 1998, 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
  • 10
    • 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
  • 12
    • 84863229364 scopus 로고    scopus 로고
    • Structure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter
    • Baglieri J., Beck D., Vasisht N., Smith C.J., Robinson C. Structure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter. J. Biol. Chem. 2012, 287:7335-7344.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7335-7344
    • Baglieri, J.1    Beck, D.2    Vasisht, N.3    Smith, C.J.4    Robinson, C.5
  • 13
    • 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.L., 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.L.4    Robinson, C.5
  • 15
    • 12344296658 scopus 로고    scopus 로고
    • The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex
    • Oates J., Barrett C.M.L., Barnett J.P., Byrne K.G., Bolhuis A., Robinson C. The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex. J. Mol. Biol. 2005, 346:295-305.
    • (2005) J. Mol. Biol. , vol.346 , pp. 295-305
    • Oates, J.1    Barrett, C.M.L.2    Barnett, J.P.3    Byrne, K.G.4    Bolhuis, A.5    Robinson, C.6
  • 16
    • 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
  • 20
    • 84863731293 scopus 로고    scopus 로고
    • TatAc, the third TatA subunit of Bacillus subtilis, can form active twin-arginine translocases with the TatCd and TatCy subunits
    • Monteferrante C.G., Baglieri J., Robinson C., van Dijl J.M. TatAc, the third TatA subunit of Bacillus subtilis, can form active twin-arginine translocases with the TatCd and TatCy subunits. Appl. Environ. Microbiol. 2012, 78:4999-5001.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 4999-5001
    • Monteferrante, C.G.1    Baglieri, J.2    Robinson, C.3    van Dijl, J.M.4
  • 22
    • 0036479116 scopus 로고    scopus 로고
    • The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system
    • Pop O., Martin U., Abel C., Muller J.P. The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system. J. Biol. Chem. 2002, 277:3268-3273.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3268-3273
    • Pop, O.1    Martin, U.2    Abel, C.3    Muller, J.P.4
  • 24
    • 41449118764 scopus 로고    scopus 로고
    • A minimal Tat system from a Gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes
    • Barnett J.P., Eijlander R.T., Kuipers O.P., Robinson C. A minimal Tat system from a Gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J. Biol. Chem. 2008, 283:2534-2542.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2534-2542
    • Barnett, J.P.1    Eijlander, R.T.2    Kuipers, O.P.3    Robinson, C.4
  • 25
    • 57649142832 scopus 로고    scopus 로고
    • The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements
    • Barnett J.P., van der Ploeg R., Eijlander R.T., Nenninger A., Mendel S., Rozeboom R., Kuipers O.P., van Dijl J.M., Robinson C. The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements. FEBS J. 2009, 276:232-243.
    • (2009) FEBS J. , vol.276 , pp. 232-243
    • Barnett, J.P.1    van der Ploeg, R.2    Eijlander, R.T.3    Nenninger, A.4    Mendel, S.5    Rozeboom, R.6    Kuipers, O.P.7    van Dijl, J.M.8    Robinson, C.9
  • 27
    • 0037274388 scopus 로고    scopus 로고
    • An alternative model of the twin arginine translocation system
    • Brüser T., Sanders C. An alternative model of the twin arginine translocation system. Microbiol. Res. 2003, 158:7-17.
    • (2003) Microbiol. Res. , vol.158 , pp. 7-17
    • Brüser, T.1    Sanders, C.2
  • 29
    • 0024388691 scopus 로고
    • The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers
    • Silvestro A., Pommier J., Pascal M.C., Giordano G. The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers. Biochim. Biophys. Acta 1989, 999:208-216.
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 208-216
    • Silvestro, A.1    Pommier, J.2    Pascal, M.C.3    Giordano, G.4
  • 30
    • 33947180023 scopus 로고    scopus 로고
    • Structural analysis of membrane protein complexes by single particle electron microscopy
    • Rubinstein J.L. Structural analysis of membrane protein complexes by single particle electron microscopy. Methods 2007, 41:409-416.
    • (2007) Methods , vol.41 , pp. 409-416
    • Rubinstein, J.L.1
  • 31
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 1996, 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 32
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh T.R., Gao H., Baxter W.T., Asturias F.J., Boisset N., Leith A., Frank J. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 2008, 3:1941-1974.
    • (2008) Nat. Protoc. , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5    Leith, A.6    Frank, J.7
  • 33
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell J., Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 2003, 142:334-347.
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.1    Grigorieff, N.2
  • 34
    • 0742272143 scopus 로고    scopus 로고
    • Recognition and separation of single particles with size variation by statistical analysis of their images
    • White H.E., Saibil H.R., Ignatiou A., Orlova E.V. Recognition and separation of single particles with size variation by statistical analysis of their images. J. Mol. Biol. 2004, 336:453-460.
    • (2004) J. Mol. Biol. , vol.336 , pp. 453-460
    • White, H.E.1    Saibil, H.R.2    Ignatiou, A.3    Orlova, E.V.4
  • 35
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P., Radermacher M., Frank J. Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 1992, 40:33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 36
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M., Wagenknecht T., Verschoor A., Frank J. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 1987, 146:113-136.
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 37
    • 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
  • 39
    • 65249161748 scopus 로고    scopus 로고
    • Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system
    • Dabney-Smith C., Cline K. Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system. Mol. Biol. Cell 2009, 20:2060-2069.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2060-2069
    • Dabney-Smith, C.1    Cline, K.2
  • 41
    • 34948880704 scopus 로고    scopus 로고
    • Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach
    • Lange C., Müller S.D., Walther T.H., Bürck J., Ulrich A.S. Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach. Biochim. Biophys. Acta Biomembr. 2007, 1768:2627-2634.
    • (2007) Biochim. Biophys. Acta Biomembr. , vol.1768 , pp. 2627-2634
    • Lange, C.1    Müller, S.D.2    Walther, T.H.3    Bürck, J.4    Ulrich, A.S.5
  • 42
    • 78449242888 scopus 로고    scopus 로고
    • Membrane alignment of the pore-forming component TatAd 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 TatAd 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
  • 43
    • 1642523788 scopus 로고    scopus 로고
    • Dual topology of the Escherichia coli TatA protein
    • Gouffi K., Gérard F., Santini C.-L., Wu L.-F. Dual topology of the Escherichia coli TatA protein. J. Biol. Chem. 2004, 279:11608-11615.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11608-11615
    • Gouffi, K.1    Gérard, F.2    Santini, C.-L.3    Wu, L.-F.4
  • 45
    • 70349481163 scopus 로고    scopus 로고
    • Structure analysis of the membrane protein TatCd from the Tat system of B. subtilis by circular dichroism
    • Nolandt O.V., Walther T.H., Roth S., Bürck J., Ulrich A.S. Structure analysis of the membrane protein TatCd from the Tat system of B. subtilis by circular dichroism. Biochim. Biophys. Acta Biomembr. 2009, 1788:2238-2244.
    • (2009) Biochim. Biophys. Acta Biomembr. , vol.1788 , pp. 2238-2244
    • Nolandt, O.V.1    Walther, T.H.2    Roth, S.3    Bürck, J.4    Ulrich, A.S.5
  • 46
    • 0033579428 scopus 로고    scopus 로고
    • Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein
    • Sargent F., Stanley N.R., Berks B.C., Palmer T. Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein. J. Biol. Chem. 1999, 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


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