메뉴 건너뛰기




Volumn 355, Issue 5, 2006, Pages 957-967

Unassisted membrane insertion as the initial step in ΔpH/Tat- dependent protein transport

Author keywords

Protein transport; Tat pathway; Thylakoid membrane; Translocation intermediate; Twin arginine

Indexed keywords

LIPOSOME; TRANSACTIVATOR PROTEIN;

EID: 29444443773     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.029     Document Type: Article
Times cited : (54)

References (51)
  • 1
    • 0035852327 scopus 로고    scopus 로고
    • Post-translational protein translocation into thylakoids by the Sec and ΔpH-dependent pathways
    • H. Mori, and K. Cline Post-translational protein translocation into thylakoids by the Sec and ΔpH-dependent pathways Biochim. Biophys. Acta 1541 2001 80 90
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 80-90
    • Mori, H.1    Cline, K.2
  • 2
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • C. Robinson, and A. Bolhuis Tat-dependent protein targeting in prokaryotes and chloroplasts Biochim. Biophys. Acta 1694 2004 135 147
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 135-147
    • Robinson, C.1    Bolhuis, A.2
  • 3
    • 18844442890 scopus 로고    scopus 로고
    • The Tat pathway in bacteria and chloroplasts
    • M. Müller, and R.B. Klösgen The Tat pathway in bacteria and chloroplasts Mol. Membr. Biol. 22 2005 113 121
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 113-121
    • Müller, M.1    Klösgen, R.B.2
  • 4
    • 0029079118 scopus 로고
    • A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the ΔpH-dependent thylakoidal protein translocase
    • A.M. Chaddock, A. Mant, I. Karnauchov, S. Brink, R.G. Herrmann, R.B. Klösgen, and C. Robinson A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the ΔpH-dependent thylakoidal protein translocase EMBO J. 14 1995 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
  • 5
    • 0026050854 scopus 로고
    • Transport of proteins into chloroplasts. Requirements for the efficient import of two lumenal oxygen-evolving complex proteins into isolated thylakoids
    • R.M. Mould, J.B. Shackleton, and C. Robinson Transport of proteins into chloroplasts. Requirements for the efficient import of two lumenal oxygen-evolving complex proteins into isolated thylakoids J. Biol. Chem. 266 1991 17286 17289
    • (1991) J. Biol. Chem. , vol.266 , pp. 17286-17289
    • Mould, R.M.1    Shackleton, J.B.2    Robinson, C.3
  • 6
    • 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
    • K. Cline, W.F. Ettinger, and S.M. Theg 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 1992 2688 2696
    • (1992) J. Biol. Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 7
    • 0026828029 scopus 로고
    • Proton gradient-driven import of the 16 kDa oxygen-evolving complex protein as the full precursor protein by isolated thylakoids
    • R.B. Klösgen, I.A. Brock, R.G. Herrmann, and C. Robinson Proton gradient-driven import of the 16 kDa oxygen-evolving complex protein as the full precursor protein by isolated thylakoids Plant Mol. Biol. 18 1992 1031 1034
    • (1992) Plant Mol. Biol. , vol.18 , pp. 1031-1034
    • Klösgen, R.B.1    Brock, I.A.2    Herrmann, R.G.3    Robinson, C.4
  • 8
    • 0037462475 scopus 로고    scopus 로고
    • Energetics of protein transport across biological membranes. a study of the thylakoid ΔpH-dependent/cpTat pathway
    • N.N. Alder, and S.M. Theg Energetics of protein transport across biological membranes. A study of the thylakoid ΔpH-dependent/cpTat pathway Cell 112 2003 231 242
    • (2003) Cell , vol.112 , pp. 231-242
    • Alder, N.N.1    Theg, S.M.2
  • 9
    • 0037450644 scopus 로고    scopus 로고
    • Thylakoid targeting of Tat passenger proteins shows no ΔpH dependence in vivo
    • G. Finazzi, C. Chasen, F.A. Wollman, and C. de Vitry Thylakoid targeting of Tat passenger proteins shows no ΔpH dependence in vivo EMBO J. 22 2003 807 815
    • (2003) EMBO J. , vol.22 , pp. 807-815
    • Finazzi, G.1    Chasen, C.2    Wollman, F.A.3    De Vitry, C.4
  • 10
    • 16344367899 scopus 로고    scopus 로고
    • The energetics of the chloroplast Tat protein transport pathway revisited
    • S.M. Theg, K. Cline, G. Finazzi, and F.A. Wollman The energetics of the chloroplast Tat protein transport pathway revisited Trends Plant. Sci. 10 2005 153 154
    • (2005) Trends Plant. Sci. , vol.10 , pp. 153-154
    • Theg, S.M.1    Cline, K.2    Finazzi, G.3    Wollman, F.A.4
  • 11
    • 0030918441 scopus 로고    scopus 로고
    • A folded protein can be transported across the chloroplast envelope and thylakoid membranes
    • S.A. Clark, and S.M. Theg A folded protein can be transported across the chloroplast envelope and thylakoid membranes Mol. Biol. Cell 8 1997 923 934
    • (1997) Mol. Biol. Cell , vol.8 , pp. 923-934
    • Clark, S.A.1    Theg, S.M.2
  • 12
    • 0032567332 scopus 로고    scopus 로고
    • The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane
    • P.J. Hynds, D. Robinson, and C. Robinson The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane J. Biol. Chem. 273 1998 34868 34874
    • (1998) J. Biol. Chem. , vol.273 , pp. 34868-34874
    • Hynds, P.J.1    Robinson, D.2    Robinson, C.3
  • 14
    • 4043075625 scopus 로고    scopus 로고
    • In vivo transport of folded EGFP by the ΔpH/TAT-dependent pathway in chloroplasts of Arabidopsis thaliana
    • J.P. Marques, M.H. Schattat, G. Hause, I. Dudeck, and R.B. Klösgen In vivo transport of folded EGFP by the ΔpH/TAT-dependent pathway in chloroplasts of Arabidopsis thaliana J. Expt. Bot. 55 2004 1697 1706
    • (2004) J. Expt. Bot. , vol.55 , pp. 1697-1706
    • Marques, J.P.1    Schattat, M.H.2    Hause, G.3    Dudeck, I.4    Klösgen, R.B.5
  • 16
    • 0032746027 scopus 로고    scopus 로고
    • The maize tha4 gene functions in sec-independent protein transport in chloroplasts and is related to hcf106, tatA, and tatB
    • M.B. Walker, L.M. Roy, E. Coleman, R. Voelker, and A. Barkan The maize tha4 gene functions in sec-independent protein transport in chloroplasts and is related to hcf106, tatA, and tatB J. Cell. Biol. 147 1999 267 276
    • (1999) J. Cell. Biol. , vol.147 , pp. 267-276
    • Walker, M.B.1    Roy, L.M.2    Coleman, E.3    Voelker, R.4    Barkan, A.5
  • 17
    • 0035964205 scopus 로고    scopus 로고
    • An essential role of a TatC homologue of a Delta pH- dependent protein transporter in thylakoid membrane formation during chloroplast development in Arabidopsis thaliana
    • R. Motohashi, N. Nagata, T. Ito, S. Takahashi, T. Hobo, S. Yoshida, and K. Shinozaki An essential role of a TatC homologue of a Delta pH- dependent protein transporter in thylakoid membrane formation during chloroplast development in Arabidopsis thaliana Proc. Natl Acad. Sci. USA 98 2001 10499 10504
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10499-10504
    • Motohashi, R.1    Nagata, N.2    Ito, T.3    Takahashi, S.4    Hobo, T.5    Yoshida, S.6    Shinozaki, K.7
  • 18
    • 0242444212 scopus 로고    scopus 로고
    • Two distinct translocation intermediates can be distinguished during protein transport by the TAT (ΔpH)-pathway across the thylakoid membrane
    • J. Berghöfer, and R.B. Klösgen Two distinct translocation intermediates can be distinguished during protein transport by the TAT (ΔpH)-pathway across the thylakoid membrane FEBS Letters 460 1999 328 332
    • (1999) FEBS Letters , vol.460 , pp. 328-332
    • Berghöfer, J.1    Klösgen, R.B.2
  • 19
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • K. Cline, and H. Mori Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport J. Cell Biol. 154 2001 719 729
    • (2001) J. Cell Biol. , vol.154 , pp. 719-729
    • Cline, K.1    Mori, H.2
  • 20
    • 0037092039 scopus 로고    scopus 로고
    • A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
    • H. Mori, and K. Cline A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase J. Cell Biol. 157 2002 205 210
    • (2002) J. Cell Biol. , vol.157 , pp. 205-210
    • Mori, H.1    Cline, K.2
  • 21
    • 15744405122 scopus 로고    scopus 로고
    • Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
    • B.C. Berks, T. Palmer, and F. Sargent Protein targeting by the bacterial twin-arginine translocation (Tat) pathway Curr. Opin. Microbiol. 8 2005 174 181
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 174-181
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 22
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • B.C. Berks A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22 1996 393 404
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 23
    • 0037352234 scopus 로고    scopus 로고
    • Moving folded proteins across the bacterial cell membrane
    • T. Palmer, and B.C. Berks Moving folded proteins across the bacterial cell membrane Microbiology 149 2003 547 556
    • (2003) Microbiology , vol.149 , pp. 547-556
    • Palmer, T.1    Berks, B.C.2
  • 24
    • 0032512709 scopus 로고    scopus 로고
    • Evidence for a loop mechanism of protein transport by the thylakoid Delta pH pathway
    • V. Fincher, M. McCaffery, and K. Cline Evidence for a loop mechanism of protein transport by the thylakoid Delta pH pathway FEBS Letters 423 1998 66 70
    • (1998) FEBS Letters , vol.423 , pp. 66-70
    • Fincher, V.1    McCaffery, M.2    Cline, K.3
  • 25
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • M. Alami, I. Luke, S. Deitermann, G. Eisner, H.G. Koch, J. Brunner, and M. Müller Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli Mol. Cell 12 2003 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    Müller, M.7
  • 26
    • 0033549567 scopus 로고    scopus 로고
    • Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways
    • H. Mori, E.J. Summer, X. Ma, and K. Cline Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways J. Cell Biol. 146 1999 45 56
    • (1999) J. Cell Biol. , vol.146 , pp. 45-56
    • Mori, H.1    Summer, E.J.2    Ma, X.3    Cline, K.4
  • 27
    • 2442543556 scopus 로고    scopus 로고
    • Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
    • K. Ifuku, T. Nakatsu, H. Kato, and F. Sato Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum EMBO Rep. 5 2004 362 367
    • (2004) EMBO Rep. , vol.5 , pp. 362-367
    • Ifuku, K.1    Nakatsu, T.2    Kato, H.3    Sato, F.4
  • 29
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • A.P. Pugsley The complete general secretory pathway in Gram-negative bacteria Microbiol. Rev. 57 1993 50 108
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 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
    • N.R. Stanley, T. Palmer, and B.C. Berks The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli J. Biol. Chem. 275 2000 11591 11596
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 31
    • 0034031057 scopus 로고    scopus 로고
    • Characterization of the early steps of OE17 precursor transport by the thylakoid ΔpH/Tat machinery
    • S.M. Musser, and S.M. Theg Characterization of the early steps of OE17 precursor transport by the thylakoid ΔpH/Tat machinery Eur. J. Biochem. 267 2000 2588 2598
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2588-2598
    • Musser, S.M.1    Theg, S.M.2
  • 32
    • 0028261428 scopus 로고
    • Targeting of proteins to the thylakoids by bipartite presequences: CFoII is imported by a novel, third pathway
    • D. Michl, C. Robinson, J.B. Shackleton, R.G. Herrmann, and R.B. Klösgen Targeting of proteins to the thylakoids by bipartite presequences: CFoII is imported by a novel, third pathway EMBO J. 13 1994 1310 1317
    • (1994) EMBO J. , vol.13 , pp. 1310-1317
    • Michl, D.1    Robinson, C.2    Shackleton, J.B.3    Herrmann, R.G.4    Klösgen, R.B.5
  • 33
    • 0030512497 scopus 로고    scopus 로고
    • Protease-sensitive thylakoidal import machinery for the Sec-ΔpH- and signal recognition particle-dependent protein targeting pathways, but not for CFo-II integration
    • D. Robinson, I. Karnauchov, R.G. Herrmann, R.B. Klösgen, and C. Robinson Protease-sensitive thylakoidal import machinery for the Sec-ΔpH- and signal recognition particle-dependent protein targeting pathways, but not for CFo-II integration Plant J. 10 1996 149 155
    • (1996) Plant J. , vol.10 , pp. 149-155
    • Robinson, D.1    Karnauchov, I.2    Herrmann, R.G.3    Klösgen, R.B.4    Robinson, C.5
  • 34
    • 0032489422 scopus 로고    scopus 로고
    • Sec/SRP-independent insertion of two thylakoid membrane proteins bearing cleavable signal peptides
    • S.J. Kim, C. Robinson, and A. Mant Sec/SRP-independent insertion of two thylakoid membrane proteins bearing cleavable signal peptides FEBS Letters 424 1998 105 108
    • (1998) FEBS Letters , vol.424 , pp. 105-108
    • Kim, S.J.1    Robinson, C.2    Mant, A.3
  • 35
    • 0023054119 scopus 로고
    • Both hydrophobic domains of M13 procoat are required to initiate membrane insertion
    • A. Kuhn, G. Kreil, and W. Wickner Both hydrophobic domains of M13 procoat are required to initiate membrane insertion EMBO J. 5 1986 3681 3685
    • (1986) EMBO J. , vol.5 , pp. 3681-3685
    • Kuhn, A.1    Kreil, G.2    Wickner, W.3
  • 37
    • 0035860693 scopus 로고    scopus 로고
    • Function of YidC for the insertion of M13 procoat protein in Escherichia coli: Translocation of mutants that show differences in their membrane potential dependence and Sec requirement
    • J.C. Samuelson, F. Jiang, L. Yi, M. Chen, J.W. de Gier, A. Kuhn, and R.E. Dalbey Function of YidC for the insertion of M13 procoat protein in Escherichia coli: translocation of mutants that show differences in their membrane potential dependence and Sec requirement J. Biol. Chem. 276 2001 34847 34852
    • (2001) J. Biol. Chem. , vol.276 , pp. 34847-34852
    • Samuelson, J.C.1    Jiang, F.2    Yi, L.3    Chen, M.4    De Gier, J.W.5    Kuhn, A.6    Dalbey, R.E.7
  • 38
    • 0035798617 scopus 로고    scopus 로고
    • Distinct Albino3-dependent and -independent pathways for thylakoid membrane protein insertion
    • C.A. Woolhead, S.J. Thompson, M. Moore, C. Tissier, A. Mant, and A. Rodger Distinct Albino3-dependent and -independent pathways for thylakoid membrane protein insertion J. Biol. Chem. 276 2001 40841 40846
    • (2001) J. Biol. Chem. , vol.276 , pp. 40841-40846
    • Woolhead, C.A.1    Thompson, S.J.2    Moore, M.3    Tissier, C.4    Mant, A.5    Rodger, A.6
  • 39
    • 0034695557 scopus 로고    scopus 로고
    • Chloroplast Oxa1p homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes
    • M. Moore, M.S. Harrison, E.C. Peterson, and R. Henry Chloroplast Oxa1p homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes J. Biol. Chem. 275 2000 1529 1532
    • (2000) J. Biol. Chem. , vol.275 , pp. 1529-1532
    • Moore, M.1    Harrison, M.S.2    Peterson, E.C.3    Henry, R.4
  • 40
    • 0142065248 scopus 로고    scopus 로고
    • Membrane targeting of a folded and cofactor-containing protein
    • T. Brüser, T. Yano, D.C. Brune, and F. Daldal Membrane targeting of a folded and cofactor-containing protein Eur. J. Biochem. 270 2003 1211 1221
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1211-1221
    • Brüser, T.1    Yano, T.2    Brune, D.C.3    Daldal, F.4
  • 41
    • 0036274596 scopus 로고    scopus 로고
    • Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
    • G. Buchanan, E. De Leeuw, N.R. Stanley, M. Wexler, B.C. Berks, F. Sargent, and T. Palmer Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis Mol. Microbiol. 43 2002 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
  • 42
    • 18444411638 scopus 로고    scopus 로고
    • Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase
    • C.M.L. Barrett, and C. Robinson Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase FEBS J. 272 2005 2261 2275
    • (2005) FEBS J. , vol.272 , pp. 2261-2275
    • Barrett, C.M.L.1    Robinson, C.2
  • 43
    • 0027980013 scopus 로고
    • The presequence of a chimeric construct dictates which of two mechanisms are utilised for translocation across the thylakoid membrane: Evidence for the existence of two distinct translocation systems
    • C. Robinson, D. Cai, A. Hulford, I.A. Brock, D. Michl, and L. Hazell The presequence of a chimeric construct dictates which of two mechanisms are utilised for translocation across the thylakoid membrane: evidence for the existence of two distinct translocation systems EMBO J. 13 1994 279 285
    • (1994) EMBO J. , vol.13 , pp. 279-285
    • Robinson, C.1    Cai, D.2    Hulford, A.3    Brock, I.A.4    Michl, D.5    Hazell, L.6
  • 45
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • J. Seelig Thermodynamics of lipid-peptide interactions Biochim. Biophys. Acta 1666 2004 40 50
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 46
    • 0027690206 scopus 로고
    • Precursors of one integral and five lumenal thylakoid proteins are imported by isolated pea and barley thylakoids: Optimisation of in vitro assays
    • I.W. Brock, L. Hazell, D. Michl, V.S. Nielsen, B.L. Møller, and R.G. Herrmann Precursors of one integral and five lumenal thylakoid proteins are imported by isolated pea and barley thylakoids: optimisation of in vitro assays Plant Mol. Biol. 23 1993 717 725
    • (1993) Plant Mol. Biol. , vol.23 , pp. 717-725
    • Brock, I.W.1    Hazell, L.2    Michl, D.3    Nielsen, V.S.4    Møller, B.L.5    Herrmann, R.G.6
  • 47
    • 0034470076 scopus 로고    scopus 로고
    • Effect of monogalactosyldiacylglycerol and other thylakoid lipids on violaxanthin de-epoxidation in liposomes
    • D. Latowski, A. Kostecka, and K. Strzalka Effect of monogalactosyldiacylglycerol and other thylakoid lipids on violaxanthin de-epoxidation in liposomes Biochem. Soc. Trans. 28 2000 810 812
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 810-812
    • Latowski, D.1    Kostecka, A.2    Strzalka, K.3
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 50
    • 0024334643 scopus 로고
    • Luminescent immunodetection of western-blotted proteins from coomassie-stained polyacrylamide gel
    • A. Vachereau Luminescent immunodetection of western-blotted proteins from coomassie-stained polyacrylamide gel Anal. Biochem. 179 1989 206 208
    • (1989) Anal. Biochem. , vol.179 , pp. 206-208
    • Vachereau, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.