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Volumn 270, Issue 6, 2003, Pages 1211-1221

Membrane targeting of a folded and cofactor-containing protein

Author keywords

ATP dependence; High potential iron sulfur protein (HiPIP); In vitro folding; Membrane targeting; Twin arginine translocation

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE; GENOMIC DNA; IRON SULFUR PROTEIN;

EID: 0142065248     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03481.x     Document Type: Article
Times cited : (62)

References (45)
  • 1
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley, A.P. (1993) The complete general secretory pathway in Gram-negative bacteria. Microbiol. Rev. 57, 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 3
    • 0035201578 scopus 로고    scopus 로고
    • Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane
    • Müller, M., Koch, H.-G., Beck, K. & Schäfer, U. (2001) Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog. Nucleic Acid Res. 66, 107-157.
    • (2001) Prog. Nucleic Acid Res. , vol.66 , pp. 107-157
    • Müller, M.1    Koch, H.-G.2    Beck, K.3    Schäfer, U.4
  • 4
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin arginine translocation pathway
    • Robinson, C. & Bolhuis, A. (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
  • 7
    • 0034832014 scopus 로고    scopus 로고
    • Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
    • Sargent, F., Gohlke, U., de Leeuw, E., Stanley, N., Palmer, T., Saibil, H.R. & Perks, B.C. (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.4    Palmer, T.5    Saibil, H.R.6    Perks, B.C.7
  • 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., Mathers, J.E., Thomas, J.D., Barrett, C.M.L. & Robinson, C. (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.L.4    Robinson, C.5
  • 9
    • 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. (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
  • 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., Stanley, N.R., Palmer, T. & Berks, B.C. (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
    • 0040537042 scopus 로고    scopus 로고
    • Compeition between Sec- and Tat-dependent protein translocation in Escherichia coli
    • Cristóbal, S., de Gier, J.-W., Nielsen, H. & von Heijne, G. (1999) Compeition between Sec- and Tat-dependent protein translocation in Escherichia coli. EMBO J. 18, 2982-2990.
    • (1999) EMBO J. , vol.18 , pp. 2982-2990
    • Cristóbal, S.1    De Gier, J.-W.2    Nielsen, H.3    Von Heijne, G.4
  • 12
    • 0030976930 scopus 로고    scopus 로고
    • Pathway specificity for a ApH-dependent precursor thylacoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein
    • Bogsch, E., Brink, S. & Robinson, C. (1997) Pathway specificity for a ApH-dependent precursor thylacoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein. EMBO J. 16, 3851-3859.
    • (1997) EMBO J. , vol.16 , pp. 3851-3859
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 13
    • 0039351902 scopus 로고    scopus 로고
    • Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli
    • Brüser, T., Deutzmann, R. & Dahl, C. (1998) Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli. FEMS Microbiol. Lett. 164, 329-336.
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 329-336
    • Brüser, T.1    Deutzmann, R.2    Dahl, C.3
  • 14
    • 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., Bernadac, A., Zhang, A., Ize, B., Blanco, C. & Wu, L.-F. (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, A.3    Ize, B.4    Blanco, C.5    Wu, L.-F.6
  • 15
    • 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. & 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
  • 16
    • 0033532176 scopus 로고    scopus 로고
    • Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway
    • Rodrigue, A., Chanal, A., Beck, K., Müller, M. & Wu, L.-F. (1999) Co-translocation 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    Müller, M.4    Wu, L.-F.5
  • 17
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria
    • Mühlenhoff, U. & Lill, R. (2000) Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim. Biophys. Acta. 1459, 370-382.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 370-382
    • Mühlenhoff, U.1    Lill, R.2
  • 18
    • 0034944416 scopus 로고    scopus 로고
    • Transport of cytochrome c derivatives by the bacterial Tat protein translocation system
    • Sanders, C., Wethkamp, N. & Lill, H. (2001) Transport of cytochrome c derivatives by the bacterial Tat protein translocation system. Mol. Microbiol. 41, 241-246.
    • (2001) Mol. Microbiol. , vol.41 , pp. 241-246
    • Sanders, C.1    Wethkamp, N.2    Lill, H.3
  • 19
    • 0035873543 scopus 로고    scopus 로고
    • Functional reconstitution of bacterial Tat translocation in vitro
    • Yahr, T.L. & Wickner, W.T. (2001) Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 20, 1-8.
    • (2001) EMBO J. , vol.20 , pp. 1-8
    • Yahr, T.L.1    Wickner, W.T.2
  • 20
    • 0037036383 scopus 로고    scopus 로고
    • Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli
    • Alami, M., Trescher, D., Wu, L.F. & Müller, M. (2002) Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli. J. Biol. Chem. 277, 20499-20503.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20499-20503
    • Alami, M.1    Trescher, D.2    Wu, L.F.3    Müller, M.4
  • 21
    • 0016160014 scopus 로고
    • Two-Angstrom crystal structure of oxidized Chromatium high potential iron protein
    • Carter, C.W., Kraut, J., Freer, S.T., Xuong, N.-H., Alden, R.A. & Bartsch, R.G. (1974) Two-Angstrom crystal structure of oxidized Chromatium high potential iron protein. J. Biol. Chem. 249, 4212-4225.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4212-4225
    • Carter, C.W.1    Kraut, J.2    Freer, S.T.3    Xuong, N.-H.4    Alden, R.A.5    Bartsch, R.G.6
  • 22
    • 0028908669 scopus 로고
    • The three-dimensional solution structure of the reduced high-potential iron-sulphur protein from Chromatium vinosum through NMR
    • Banci, L., Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C. & Sompornpisut, P. (1995) The three-dimensional solution structure of the reduced high-potential iron-sulphur protein from Chromatium vinosum through NMR. Biochemistry 34, 206-219.
    • (1995) Biochemistry , vol.34 , pp. 206-219
    • Banci, L.1    Bertini, I.2    Dikiy, A.3    Kastrau, D.H.W.4    Luchinat, C.5    Sompornpisut, P.6
  • 23
    • 0042955484 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding the high potential iron-sulphur protein (HiPIP) from the purple sulphur bacterium Chromatium vinosum
    • Brüser, T., Trüper, H.G. & Dahl, C. (1997) Cloning and sequencing of the gene encoding the high potential iron-sulphur protein (HiPIP) from the purple sulphur bacterium Chromatium vinosum. Biochim. Biophys. Acta 1352, 18-22.
    • (1997) Biochim. Biophys. Acta , vol.1352 , pp. 18-22
    • Brüser, T.1    Trüper, H.G.2    Dahl, C.3
  • 24
    • 0030922445 scopus 로고    scopus 로고
    • Identification of a key intermediate of relevance to iron-sulphur cluster biosynthesis. Mechanism of cluster assembly and implications for protein folding
    • Natarajan, K. & Cowan, J.A. (1997) Identification of a key intermediate of relevance to iron-sulphur cluster biosynthesis. mechanism of cluster assembly and implications for protein folding. J. Am. Chem. Soc. 119, 4082-4083.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4082-4083
    • Natarajan, K.1    Cowan, J.A.2
  • 25
    • 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. (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
  • 26
    • 0034697250 scopus 로고    scopus 로고
    • Subunit interactions in the twin-arginine translocase complex of Escherichia coli
    • Bolhuis, A., Bogsch, E.G. & 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
  • 27
    • 70449202714 scopus 로고
    • Determination of serum copper and iron in a single small sample
    • Landers, J.W. & Zak, B. (1958) Determination of serum copper and iron in a single small sample. Am. J. Clin. Pathol. 29, 590-592.
    • (1958) Am. J. Clin. Pathol. , vol.29 , pp. 590-592
    • Landers, J.W.1    Zak, B.2
  • 28
    • 0037829232 scopus 로고
    • In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli
    • Müller, M. & Blobel, G. (1984) In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli. Proc. Natl Acad. Sci. USA 81, 7421-7425.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7421-7425
    • Müller, M.1    Blobel, G.2
  • 29
    • 0024523838 scopus 로고
    • Binding of a soluble factor of Escherichia coli to preproteins does not require ATP and appears to be the first step in protein export
    • Watanabe, M. & Blobel, G. (1989) Binding of a soluble factor of Escherichia coli to preproteins does not require ATP and appears to be the first step in protein export. Proc. Natl Acad. Sci. USA 86, 2248-2252.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2248-2252
    • Watanabe, M.1    Blobel, G.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 33
    • 0000633026 scopus 로고
    • High potential iron proteins: Bacterial
    • Bartsch (1971) High potential iron proteins: bacterial. Methods Enzymol. 23, 644-649.
    • (1971) Methods Enzymol , vol.23 , pp. 644-649
    • Bartsch1
  • 34
    • 0025834359 scopus 로고
    • An investigation of Chromatium vinosum high-potential iron-sulphur protein by EPR and Mossbauer spectroscopy: Evidence for a freezing-induced dimerization in NaCl solutions
    • Dunham, W.R., Hagen, W.R., Fee, J.A., Sands, R.H., Dunbar, J.B. & Humblet, C. (1991) An investigation of Chromatium vinosum high-potential iron-sulphur protein by EPR and Mossbauer spectroscopy: evidence for a freezing-induced dimerization in NaCl solutions. Biochim. Biophys. Acta 1079, 253-262.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 253-262
    • Dunham, W.R.1    Hagen, W.R.2    Fee, J.A.3    Sands, R.H.4    Dunbar, J.B.5    Humblet, C.6
  • 35
    • 0033565687 scopus 로고    scopus 로고
    • The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding
    • Halbig, D., Wiegert, T., Blaudeck, N., FreudI, R. & Sprenger, G.A. (1999) The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding. Eur. J. Biochem. 263, 543-551.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 543-551
    • Halbig, D.1    Wiegert, T.2    Blaudeck, N.3    Freudl, R.4    Sprenger, G.A.5
  • 36
    • 0027730359 scopus 로고
    • Synthesis, cloning and expression of a synthetic gene for high potential iron protein from Chromatium vinosum
    • Agarwal, A., Tan, J., Eren, M., Tevelev, A., Lui, S.M. & Cowan, J.A. (1993) Synthesis, cloning and expression of a synthetic gene for high potential iron protein from Chromatium vinosum. Biochem. Biophys. Res. Commun. 197, 1357-1362.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1357-1362
    • Agarwal, A.1    Tan, J.2    Eren, M.3    Tevelev, A.4    Lui, S.M.5    Cowan, J.A.6
  • 37
    • 0035150176 scopus 로고    scopus 로고
    • Specificity of signal peptide recognition in tat-dependent bacterial protein translocation
    • Blaudeck, N., Sprenger, G.A., Freudl, R. & Wiegert, T. (2001) Specificity of signal peptide recognition in tat-dependent bacterial protein translocation. J. Bacteriol. 183, 604-610.
    • (2001) J. Bacteriol. , vol.183 , pp. 604-610
    • Blaudeck, N.1    Sprenger, G.A.2    Freudl, R.3    Wiegert, T.4
  • 38
    • 0030747688 scopus 로고    scopus 로고
    • Characterization of a partially unfolded high potential iron protein
    • Bertini, I., Cowan, J.A., Luchinat, C., Natarajan, K. & Piccoli, M. (1997) characterization of a partially unfolded high potential iron protein. Biochemistry 36, 9332-9339.
    • (1997) Biochemistry , vol.36 , pp. 9332-9339
    • Bertini, I.1    Cowan, J.A.2    Luchinat, C.3    Natarajan, K.4    Piccoli, M.5
  • 39
    • 0027499213 scopus 로고
    • Immunogold localization of the DnaK heat shock protein in Escherichia coli cells
    • Bukau, B., Reilly, P., McCarty, J. & Walker, G.C. (1993) Immunogold localization of the DnaK heat shock protein in Escherichia coli cells. J. Gen. Microbiol. 139, 95-99.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 95-99
    • Bukau, B.1    Reilly, P.2    McCarty, J.3    Walker, G.C.4
  • 40
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik, I.J., Ladner, C.L. & Turner, R.J. (2001) Identification of a twin-arginine leader-binding protein. Mol. Microbiol. 40, 323-331.
    • (2001) Mol. Microbiol. , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 41
    • 0035029582 scopus 로고    scopus 로고
    • Biogenesis of inner membrane proteins in Escherichia coli
    • de Gier, J.-W. & Luirink, J. (2001) Biogenesis of inner membrane proteins in Escherichia coli. Mol. Microbiol. 40, 314-322.
    • (2001) Mol. Microbiol. , vol.40 , pp. 314-322
    • De Gier, J.-W.1    Luirink, J.2
  • 42
    • 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. (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    Müller, M.4    Giordano, G.5    Wu, L.-F.6
  • 43
    • 0034695557 scopus 로고    scopus 로고
    • Chloroplast Oxalp homolog Albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes
    • Moore, M., Harrison, S., Peterson, E.C. & Henry, R. (2000) Chloroplast Oxalp homolog Albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes. J. Biol. Chem. 275, 1529-1532.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1529-1532
    • Moore, M.1    Harrison, S.2    Peterson, E.C.3    Henry, R.4
  • 44
    • 0033579428 scopus 로고    scopus 로고
    • Secindependent protein translocation in Escherichia coli: A distinct and pivotal role for the TatB protein
    • Sargent, F., Stanley, N.R., Berks, B.C. & Palmer, T. (1999) Secindependent 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
  • 45
    • 0034031057 scopus 로고    scopus 로고
    • Characterization of the early steps of OE17 precursor transport by the thylakoid delta pH/Tat machinery
    • Musser, S.M. & Theg, S.M. (2000) Characterization of the early steps of OE17 precursor transport by the thylakoid delta pH/Tat machinery. Eur. J. Biochem. 267, 2588-2598.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2588-2598
    • Musser, S.M.1    Theg, S.M.2


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