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Volumn 25, Issue C, 2007, Pages 463-492

The Sec and Tat Protein Translocation Pathways in Chloroplasts

Author keywords

[No Author keywords available]

Indexed keywords

CYANOBACTERIA; ESCHERICHIA COLI;

EID: 77956694468     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6047(07)25018-8     Document Type: Chapter
Times cited : (37)

References (113)
  • 1
    • 0037213560 scopus 로고    scopus 로고
    • Chloroplast research in the genomic age
    • Leister D. Chloroplast research in the genomic age. Trends Genet 19 (2003) 47-56
    • (2003) Trends Genet , vol.19 , pp. 47-56
    • Leister, D.1
  • 4
    • 0026860017 scopus 로고
    • The chloroplast genome
    • Sugiura M. The chloroplast genome. Plant Mol Biol 19 (1992) 149-168
    • (1992) Plant Mol Biol , vol.19 , pp. 149-168
    • Sugiura, M.1
  • 5
    • 0033199778 scopus 로고    scopus 로고
    • Why have organelles retained genomes?
    • Race H.L., Herrmann R.G., and Martin W. Why have organelles retained genomes?. Trends Genet 15 (1999) 364-370
    • (1999) Trends Genet , vol.15 , pp. 364-370
    • Race, H.L.1    Herrmann, R.G.2    Martin, W.3
  • 6
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • Keegstra K., and Cline K. Protein import and routing systems of chloroplasts. Plant Cell 11 (1999) 557-570
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 7
    • 11144321346 scopus 로고    scopus 로고
    • Mechanisms of protein import and routing in chloroplasts
    • Jarvis P., and Robinson C. Mechanisms of protein import and routing in chloroplasts. Curr Biol 14 (2004) R1064-R1077
    • (2004) Curr Biol , vol.14
    • Jarvis, P.1    Robinson, C.2
  • 9
    • 0347937778 scopus 로고
    • Pathways and intermediates for the biogenesis of nuclear-encoded thylakoid proteins
    • Murata N. (Ed), Kluwer Academic Publishers, Amsterdam
    • Cline K., Henry R., Li C.-., and Yuan J. Pathways and intermediates for the biogenesis of nuclear-encoded thylakoid proteins. In: Murata N. (Ed). Research in Photosymthesis Vol. III (1992), Kluwer Academic Publishers, Amsterdam 149-156
    • (1992) Research in Photosymthesis , vol.III , pp. 149-156
    • Cline, K.1    Henry, R.2    Li, C.-.3    Yuan, J.4
  • 10
    • 0025243793 scopus 로고
    • Early events in the import/assembly pathway of an integral thylakoid protein
    • Reed J.E., Cline K., Stephens L.C., Bacot K.O., and Viitanen P.V. Early events in the import/assembly pathway of an integral thylakoid protein. Eur J Biochem 194 (1990) 33-42
    • (1990) Eur J Biochem , vol.194 , pp. 33-42
    • Reed, J.E.1    Cline, K.2    Stephens, L.C.3    Bacot, K.O.4    Viitanen, P.V.5
  • 11
    • 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. A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J Biol Chem 266 (1991) 12189-12193
    • (1991) J Biol Chem , vol.266 , pp. 12189-12193
    • Mould, R.M.1    Robinson, C.2
  • 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. 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
  • 13
    • 0023041137 scopus 로고
    • Energy dependence of protein translocation into chloroplasts
    • Flugge U.I., and Hinz G. Energy dependence of protein translocation into chloroplasts. Eur J Biochem 160 (1986) 563-570
    • (1986) Eur J Biochem , vol.160 , pp. 563-570
    • Flugge, U.I.1    Hinz, G.2
  • 14
    • 0028290813 scopus 로고
    • Differences between lumen targeting domains of chloroplast transit peptides determine pathway specificity for thylakoid transport
    • Henry R., Kapazoglou A., McCaffery M., and Cline K. Differences between lumen targeting domains of chloroplast transit peptides determine pathway specificity for thylakoid transport. J Biol Chem 269 (1994) 10189-10192
    • (1994) J Biol Chem , vol.269 , pp. 10189-10192
    • Henry, R.1    Kapazoglou, A.2    McCaffery, M.3    Cline, K.4
  • 15
    • 0028365045 scopus 로고
    • The secA inhibitor, azide, reversibly blocks the translocation of a subset of proteins across the chloroplast thylakoid membrane
    • Knott T.G., and Robinson C. The secA inhibitor, azide, reversibly blocks the translocation of a subset of proteins across the chloroplast thylakoid membrane. J Biol Chem 269 (1994) 7843-7846
    • (1994) J Biol Chem , vol.269 , pp. 7843-7846
    • Knott, T.G.1    Robinson, C.2
  • 16
    • 0027494820 scopus 로고
    • Multiple pathways for protein transport into or across the thylakoid membrane
    • Cline K., Henry R., Li C., and Yuan J. Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J 12 (1993) 4105-4114
    • (1993) EMBO J , vol.12 , pp. 4105-4114
    • Cline, K.1    Henry, R.2    Li, C.3    Yuan, J.4
  • 17
    • 0027968903 scopus 로고
    • Two distinct mechanisms for the translocation of proteins across the thylakoid membrane, one requiring the presence of a stromal protein factor and nucleotide triphosphates
    • Hulford A., Hazell L., Mould R.M., and Robinson C. Two distinct mechanisms for the translocation of proteins across the thylakoid membrane, one requiring the presence of a stromal protein factor and nucleotide triphosphates. J Biol Chem 269 (1994) 3251-3256
    • (1994) J Biol Chem , vol.269 , pp. 3251-3256
    • Hulford, A.1    Hazell, L.2    Mould, R.M.3    Robinson, C.4
  • 18
    • 0027961026 scopus 로고
    • SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting
    • Yuan J., Henry R., McCaffery M., and Cline K. SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting. Science 266 (1994) 796-798
    • (1994) Science , vol.266 , pp. 796-798
    • Yuan, J.1    Henry, R.2    McCaffery, M.3    Cline, K.4
  • 19
    • 0027944148 scopus 로고
    • Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport
    • Nakai M., Goto A., Nohara T., Sugita D., and Endo T. Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J Biol Chem 269 (1994) 31338-31341
    • (1994) J Biol Chem , vol.269 , pp. 31338-31341
    • Nakai, M.1    Goto, A.2    Nohara, T.3    Sugita, D.4    Endo, T.5
  • 20
    • 0347420178 scopus 로고    scopus 로고
    • Biogenesis of green plant thylakoid membranes
    • Green B., and Panson W. (Eds), Kluwer Academic Publishers, Dordrecht
    • Cline K. Biogenesis of green plant thylakoid membranes. In: Green B., and Panson W. (Eds). Light-Harvesting Antennas in Photosynthesis. Advances in Photosynthesis and Respiration Vol. 13 (2003), Kluwer Academic Publishers, Dordrecht 353-372
    • (2003) Light-Harvesting Antennas in Photosynthesis. Advances in Photosynthesis and Respiration , vol.13 , pp. 353-372
    • Cline, K.1
  • 21
    • 0035900736 scopus 로고    scopus 로고
    • The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: missing link in the evolution of protein transport pathways in chloroplasts?
    • Molik S., Karnauchov I., Weidlich C., Herrmann R.G., and Klosgen R.B. The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: missing link in the evolution of protein transport pathways in chloroplasts?. J Biol Chem 276 (2001) 42761-42766
    • (2001) J Biol Chem , vol.276 , pp. 42761-42766
    • Molik, S.1    Karnauchov, I.2    Weidlich, C.3    Herrmann, R.G.4    Klosgen, R.B.5
  • 22
    • 0034604535 scopus 로고    scopus 로고
    • The thylakoid delta pH-dependent pathway machinery facilitates RR-independent N-tail protein integration
    • Summer E.J., Mori H., Settles A.M., and Cline K. The thylakoid delta pH-dependent pathway machinery facilitates RR-independent N-tail protein integration. J Biol Chem 275 (2000) 23483-23490
    • (2000) J Biol Chem , vol.275 , pp. 23483-23490
    • Summer, E.J.1    Mori, H.2    Settles, A.M.3    Cline, K.4
  • 23
    • 0029731659 scopus 로고    scopus 로고
    • Import and routing of nucleus-encoded chloroplast proteins
    • Cline K., and Henry R. Import and routing of nucleus-encoded chloroplast proteins. Annu Rev Cell Dev Biol 12 (1996) 1-26
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 1-26
    • Cline, K.1    Henry, R.2
  • 24
    • 0035852327 scopus 로고    scopus 로고
    • Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways
    • Mori H., and Cline K. Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways. Biochim Biophys Acta 1541 (2001) 80-90
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 80-90
    • Mori, H.1    Cline, K.2
  • 25
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • Robinson C., and Bolhuis A. 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
  • 26
    • 0031035488 scopus 로고    scopus 로고
    • Targeting determinants and proposed evolutionary basis for the Sec and the Delta pH protein transport systems in chloroplast thylakoid membranes
    • Henry R., Carrigan M., McCaffrey M., Ma X., and Cline K. Targeting determinants and proposed evolutionary basis for the Sec and the Delta pH protein transport systems in chloroplast thylakoid membranes. J Cell Biol 136 (1997) 823-832
    • (1997) J Cell Biol , vol.136 , pp. 823-832
    • Henry, R.1    Carrigan, M.2    McCaffrey, M.3    Ma, X.4    Cline, K.5
  • 27
    • 0034616387 scopus 로고    scopus 로고
    • Precursors bind to specific sites on thylakoid membranes prior to transport on the delta pH protein translocation system
    • Ma X., and Cline K. Precursors bind to specific sites on thylakoid membranes prior to transport on the delta pH protein translocation system. J Biol Chem 275 (2000) 10016-10022
    • (2000) J Biol Chem , vol.275 , pp. 10016-10022
    • Ma, X.1    Cline, K.2
  • 28
    • 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., Klosgen R.B., and 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 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    Klosgen, R.B.6    Robinson, C.7
  • 29
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • Cline K., and Mori H. Thylakoid DeltapH-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
  • 30
    • 0037431011 scopus 로고    scopus 로고
    • Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate
    • Alder N.N., and Theg S.M. Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate. FEBS Lett 540 (2003) 96-100
    • (2003) FEBS Lett , vol.540 , pp. 96-100
    • Alder, N.N.1    Theg, S.M.2
  • 31
    • 0030976930 scopus 로고    scopus 로고
    • Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein
    • Bogsch E., Brink S., and Robinson C. Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein. EMBO J 16 (1997) 3851-3859
    • (1997) EMBO J , vol.16 , pp. 3851-3859
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 32
    • 0027238554 scopus 로고
    • Protein import into chloroplasts. The hydrophilic lumenal proteins exhibit unexpected import and sorting specificities in spite of structurally conserved transit peptides
    • Clausmeyer S., Klosgen R.B., and Herrmann R.G. Protein import into chloroplasts. The hydrophilic lumenal proteins exhibit unexpected import and sorting specificities in spite of structurally conserved transit peptides. J Biol Chem 268 (1993) 13869-13876
    • (1993) J Biol Chem , vol.268 , pp. 13869-13876
    • Clausmeyer, S.1    Klosgen, R.B.2    Herrmann, R.G.3
  • 34
    • 2942709808 scopus 로고    scopus 로고
    • The archaeal Sec-dependent protein translocation pathway
    • Bolhuis A. The archaeal Sec-dependent protein translocation pathway. Philos Trans R Soc Lond B Biol Sci 359 (2004) 919-927
    • (2004) Philos Trans R Soc Lond B Biol Sci , vol.359 , pp. 919-927
    • Bolhuis, A.1
  • 36
    • 8844261812 scopus 로고    scopus 로고
    • Sec-translocase mediated membrane protein biogenesis
    • Dalbey R.E., and Chen M. Sec-translocase mediated membrane protein biogenesis. Biochim Biophys Acta 1694 (2004) 37-53
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 37-53
    • Dalbey, R.E.1    Chen, M.2
  • 37
    • 4444290475 scopus 로고    scopus 로고
    • Structure and function of SecA, the preprotein translocase nanomotor
    • Vrontou E., and Economou A. Structure and function of SecA, the preprotein translocase nanomotor. Biochim Biophys Acta 1694 (2004) 67-80
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 67-80
    • Vrontou, E.1    Economou, A.2
  • 39
    • 0036809395 scopus 로고    scopus 로고
    • SecB, one small chaperone in the complex milieu of the cell
    • Randall L.L., and Hardy S.J. SecB, one small chaperone in the complex milieu of the cell. Cell Mol Life Sci 59 (2002) 1617-1623
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1617-1623
    • Randall, L.L.1    Hardy, S.J.2
  • 40
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion?
    • Kuhn A., Stuart R., Henry R., and Dalbey R.E. The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion?. Trends Cell Biol 13 (2003) 510-516
    • (2003) Trends Cell Biol , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.E.4
  • 41
    • 33745207364 scopus 로고    scopus 로고
    • A second thylakoid membrane-localized Alb3/OxaI/YidC homologue is involved in proper chloroplast biogenesis in Arabidopsis thaliana
    • Gerdes L., Bals T., Klostermann E., Karl M., Philippar K., Hunken M., Soll J., and Schunemann D. A second thylakoid membrane-localized Alb3/OxaI/YidC homologue is involved in proper chloroplast biogenesis in Arabidopsis thaliana. J Biol Chem 281 (2006) 16632-16642
    • (2006) J Biol Chem , vol.281 , pp. 16632-16642
    • Gerdes, L.1    Bals, T.2    Klostermann, E.3    Karl, M.4    Philippar, K.5    Hunken, M.6    Soll, J.7    Schunemann, D.8
  • 42
    • 0030817507 scopus 로고    scopus 로고
    • Chloroplast SecA functions as a membrane-associated component of the Sec-like protein translocase of pea chloroplasts
    • Haward S.R., Napier J.A., and Gray J.C. Chloroplast SecA functions as a membrane-associated component of the Sec-like protein translocase of pea chloroplasts. Eur J Biochem 248 (1997) 724-730
    • (1997) Eur J Biochem , vol.248 , pp. 724-730
    • Haward, S.R.1    Napier, J.A.2    Gray, J.C.3
  • 44
    • 0033549567 scopus 로고    scopus 로고
    • Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways
    • Mori H., Summer E.J., Ma X., and Cline K. 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
  • 45
    • 0028227857 scopus 로고
    • Plastocyanin and the 33-kDa subunit of the oxygen-evolving complex are transported into thylakoids with similar requirements as predicted from pathway specificity
    • Yuan J., and Cline K. Plastocyanin and the 33-kDa subunit of the oxygen-evolving complex are transported into thylakoids with similar requirements as predicted from pathway specificity. J Biol Chem 269 (1994) 18463-18467
    • (1994) J Biol Chem , vol.269 , pp. 18463-18467
    • Yuan, J.1    Cline, K.2
  • 46
    • 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. 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
  • 47
    • 0028017537 scopus 로고
    • Chloroplast protein import. Chloroplast envelopes and thylakoids have different abilities to unfold proteins
    • Endo T., Kawakami M., Goto A., America T., Weisbeek P., and Nakai M. Chloroplast protein import. Chloroplast envelopes and thylakoids have different abilities to unfold proteins. Eur J Biochem 225 (1994) 403-409
    • (1994) Eur J Biochem , vol.225 , pp. 403-409
    • Endo, T.1    Kawakami, M.2    Goto, A.3    America, T.4    Weisbeek, P.5    Nakai, M.6
  • 48
    • 0030961571 scopus 로고    scopus 로고
    • Assembly of newly imported oxygen-evolving complex subunits in isolated chloroplasts: sites of assembly and mechanism of binding
    • Hashimoto A., Ettinger W.F., Yamamoto Y., and Theg S.M. Assembly of newly imported oxygen-evolving complex subunits in isolated chloroplasts: sites of assembly and mechanism of binding. Plant Cell 9 (1997) 441-452
    • (1997) Plant Cell , vol.9 , pp. 441-452
    • Hashimoto, A.1    Ettinger, W.F.2    Yamamoto, Y.3    Theg, S.M.4
  • 49
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker R., and Barkan A. Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J 14 (1995) 3905-3914
    • (1995) EMBO J , vol.14 , pp. 3905-3914
    • Voelker, R.1    Barkan, A.2
  • 50
    • 0034817555 scopus 로고    scopus 로고
    • Assembly of cytochrome f into the cytochrome bf complex in isolated pea chloroplasts
    • Mould R.M., Kapazoglou A., and Gray J.C. Assembly of cytochrome f into the cytochrome bf complex in isolated pea chloroplasts. Eur J Biochem 268 (2001) 792-799
    • (2001) Eur J Biochem , vol.268 , pp. 792-799
    • Mould, R.M.1    Kapazoglou, A.2    Gray, J.C.3
  • 51
    • 0035929632 scopus 로고    scopus 로고
    • In vitro reconstitution of insertion and processing of cytochrome f in a homologous chloroplast translation system
    • Rohl T., and van Wijk K.J. In vitro reconstitution of insertion and processing of cytochrome f in a homologous chloroplast translation system. J Biol Chem 276 (2001) 35465-35472
    • (2001) J Biol Chem , vol.276 , pp. 35465-35472
    • Rohl, T.1    van Wijk, K.J.2
  • 53
    • 0035851097 scopus 로고    scopus 로고
    • A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis
    • Zhang L., Paakkarinen V., Suorsa M., and Aro E.M. A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis. J Biol Chem 276 (2001) 37809-37814
    • (2001) J Biol Chem , vol.276 , pp. 37809-37814
    • Zhang, L.1    Paakkarinen, V.2    Suorsa, M.3    Aro, E.M.4
  • 54
    • 0033081464 scopus 로고    scopus 로고
    • Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54
    • Nilsson R., Brunner J., Hoffman N.E., and van Wijk K.J. Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54. EMBO J 18 (1999) 733-742
    • (1999) EMBO J , vol.18 , pp. 733-742
    • Nilsson, R.1    Brunner, J.2    Hoffman, N.E.3    van Wijk, K.J.4
  • 55
    • 3142782909 scopus 로고    scopus 로고
    • Efficient assembly of photosystem II in Chlamydomonas reinhardtii requires Alb3.1p, a homolog of Arabidopsis ALBINO3
    • Ossenbuhl F., Gohre V., Meurer J., Krieger-Liszkay A., Rochaix J.D., and Eichacker L.A. Efficient assembly of photosystem II in Chlamydomonas reinhardtii requires Alb3.1p, a homolog of Arabidopsis ALBINO3. Plant Cell 16 (2004) 1790-1800
    • (2004) Plant Cell , vol.16 , pp. 1790-1800
    • Ossenbuhl, F.1    Gohre, V.2    Meurer, J.3    Krieger-Liszkay, A.4    Rochaix, J.D.5    Eichacker, L.A.6
  • 56
    • 0037115768 scopus 로고    scopus 로고
    • The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana
    • Klostermann E., Droste Gen Helling I., Carde J.P., and Schunemann D. The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana. Biochem J 368 (2002) 777-781
    • (2002) Biochem J , vol.368 , pp. 777-781
    • Klostermann, E.1    Droste Gen Helling, I.2    Carde, J.P.3    Schunemann, D.4
  • 57
    • 0032550223 scopus 로고    scopus 로고
    • A SecY homologue is required for the elaboration of the chloroplast thylakoid membrane and for normal chloroplast gene expression
    • Roy L.M., and Barkan A. A SecY homologue is required for the elaboration of the chloroplast thylakoid membrane and for normal chloroplast gene expression. J Cell Biol 141 (1998) 385-395
    • (1998) J Cell Biol , vol.141 , pp. 385-395
    • Roy, L.M.1    Barkan, A.2
  • 58
    • 0348140629 scopus 로고    scopus 로고
    • Functional assembly of thylakoid deltapH-dependent/Tat protein transport pathway components in vitro
    • Fincher V., Dabney-Smith C., and Cline K. Functional assembly of thylakoid deltapH-dependent/Tat protein transport pathway components in vitro. Eur J Biochem 270 (2003) 4930-4941
    • (2003) Eur J Biochem , vol.270 , pp. 4930-4941
    • Fincher, V.1    Dabney-Smith, C.2    Cline, K.3
  • 59
    • 27744459930 scopus 로고    scopus 로고
    • Complete maturation of the plastid protein translocation channel requires a type I signal peptidase
    • Inoue K., Baldwin A.J., Shipman R.L., Matsui K., Theg S.M., and Ohme-Takagi M. Complete maturation of the plastid protein translocation channel requires a type I signal peptidase. J Cell Biol 171 (2005) 425-430
    • (2005) J Cell Biol , vol.171 , pp. 425-430
    • Inoue, K.1    Baldwin, A.J.2    Shipman, R.L.3    Matsui, K.4    Theg, S.M.5    Ohme-Takagi, M.6
  • 60
    • 18844400862 scopus 로고    scopus 로고
    • Protein translocation into and within cyanelles (review)
    • Steiner J.M., and Loffelhardt W. Protein translocation into and within cyanelles (review). Mol Membr Biol 22 (2005) 123-132
    • (2005) Mol Membr Biol , vol.22 , pp. 123-132
    • Steiner, J.M.1    Loffelhardt, W.2
  • 63
    • 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 22 (1996) 393-404
    • (1996) Mol Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 64
    • 0037317124 scopus 로고    scopus 로고
    • Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey
    • Dilks K., Rose R.W., Hartmann E., and Pohlschroder M. Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey. J Bacteriol 185 (2003) 1478-1483
    • (2003) J Bacteriol , vol.185 , pp. 1478-1483
    • Dilks, K.1    Rose, R.W.2    Hartmann, E.3    Pohlschroder, M.4
  • 66
    • 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., Muller M., and Wu L.F. Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway. J Biol Chem 274 (1999) 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
  • 67
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa M.P., Tullman D., and Georgiou G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc Natl Acad Sci USA 100 (2003) 6115-6120
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 68
    • 0028945041 scopus 로고
    • A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoidal protein transport pathway
    • Creighton A.M., Hulford A., Mant A., Robinson D., and Robinson C. A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoidal protein transport pathway. J Biol Chem 270 (1995) 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
  • 69
    • 0034031057 scopus 로고    scopus 로고
    • Characterization of the early steps of OE17 precursor transport by the thylakoid DeltapH/Tat machinery
    • Musser S.M., and Theg S.M. Characterization of the early steps of OE17 precursor transport by the thylakoid DeltapH/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
  • 70
    • 0030918441 scopus 로고    scopus 로고
    • A folded protein can be transported across the chloroplast envelope and thylakoid membranes
    • Clark S.A., and Theg S.M. 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
  • 71
    • 0037898431 scopus 로고    scopus 로고
    • Targeting of EGFP chimeras within chloroplasts
    • Marques J.P., Dudeck I., and Klosgen R.B. Targeting of EGFP chimeras within chloroplasts. Mol Genet Genomics 269 (2003) 381-387
    • (2003) Mol Genet Genomics , vol.269 , pp. 381-387
    • Marques, J.P.1    Dudeck, I.2    Klosgen, R.B.3
  • 72
    • 0141672034 scopus 로고    scopus 로고
    • The Tat protein translocation pathway and its role in microbial physiology
    • Berks B.C., Palmer T., and Sargent F. The Tat protein translocation pathway and its role in microbial physiology. Adv Microb Physiol 47 (2003) 187-254
    • (2003) Adv Microb Physiol , vol.47 , pp. 187-254
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 73
    • 0029846723 scopus 로고    scopus 로고
    • Analysis of the import of carboxyl-terminal truncations of the 23-kilodalton subunit of the oxygen-evolving complex suggests that its structure is an important determinant for thylakoid transport
    • Roffey R.A., and Theg S.M. Analysis of the import of carboxyl-terminal truncations of the 23-kilodalton subunit of the oxygen-evolving complex suggests that its structure is an important determinant for thylakoid transport. Plant Physiol 111 (1996) 1329-1338
    • (1996) Plant Physiol , vol.111 , pp. 1329-1338
    • Roffey, R.A.1    Theg, S.M.2
  • 74
    • 0028294931 scopus 로고
    • Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex
    • Kortt A.A., Malby R.L., Caldwell J.B., Gruen L.C., Ivancic N., Lawrence M.C., Howlett G.J., Webster R.G., Hudson P.J., and Colman P.M. Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex. Eur J Biochem 221 (1994) 151-157
    • (1994) Eur J Biochem , vol.221 , pp. 151-157
    • Kortt, A.A.1    Malby, R.L.2    Caldwell, J.B.3    Gruen, L.C.4    Ivancic, N.5    Lawrence, M.C.6    Howlett, G.J.7    Webster, R.G.8    Hudson, P.J.9    Colman, P.M.10
  • 75
    • 0032539535 scopus 로고    scopus 로고
    • Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation
    • Teter S.A., and Theg S.M. Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation. Proc Natl Acad Sci USA 95 (1998) 1590-1594
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1590-1594
    • Teter, S.A.1    Theg, S.M.2
  • 76
    • 0037462475 scopus 로고    scopus 로고
    • Energetics of protein transport across biological membranes: a study of the thylakoid DeltapH-dependent/cpTat pathway
    • Alder N.N., and Theg S.M. Energetics of protein transport across biological membranes: a study of the thylakoid DeltapH-dependent/cpTat pathway. Cell 112 (2003) 231-242
    • (2003) Cell , vol.112 , pp. 231-242
    • Alder, N.N.1    Theg, S.M.2
  • 77
    • 0037450644 scopus 로고    scopus 로고
    • Thylakoid targeting of Tat passenger proteins shows no delta pH dependence in vivo
    • Finazzi G., Chasen C., Wollman F.A., and de Vitry C. Thylakoid targeting of Tat passenger proteins shows no delta pH 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
  • 78
    • 16344367899 scopus 로고    scopus 로고
    • The energetics of the chloroplast Tat protein transport pathway revisited
    • Theg S.M., Cline K., Finazzi G., and Wollman F.A. 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
  • 79
    • 29244476252 scopus 로고    scopus 로고
    • The thylakoid delta pH/delta psi are not required for the initial stages of Tat-dependent protein transport in tobacco protoplasts
    • Di Cola A., Bailey S., and Robinson C. The thylakoid delta pH/delta psi are not required for the initial stages of Tat-dependent protein transport in tobacco protoplasts. J Biol Chem 280 (2005) 41165-41170
    • (2005) J Biol Chem , vol.280 , pp. 41165-41170
    • Di Cola, A.1    Bailey, S.2    Robinson, C.3
  • 80
    • 0029558120 scopus 로고
    • Relationship between photosynthetic electron transport and pH gradient across the thylakoid membrane in intact leaves
    • Schonknecht G., Neimanis S., Katona E., Gerst U., and Heber U. Relationship between photosynthetic electron transport and pH gradient across the thylakoid membrane in intact leaves. Proc Natl Acad Sci USA 92 (1995) 12185-12189
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12185-12189
    • Schonknecht, G.1    Neimanis, S.2    Katona, E.3    Gerst, U.4    Heber, U.5
  • 81
    • 0040862949 scopus 로고
    • + -atpase in intact chloroplasts
    • + -atpase in intact chloroplasts. Plant Physiol 70 (1982) 87-91
    • (1982) Plant Physiol , vol.70 , pp. 87-91
    • Shahak, Y.1
  • 83
    • 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. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J 17 (1998) 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
  • 84
  • 85
    • 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. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J Biol Chem 273 (1998) 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
  • 86
    • 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
    • Walker M.B., Roy L.M., Coleman E., Voelker R., and Barkan A. 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
  • 87
    • 0035854799 scopus 로고    scopus 로고
    • Chloroplast TatC plays a direct role in thylakoid (Delta)pH-dependent protein transport
    • Mori H., Summer E.J., and Cline K. Chloroplast TatC plays a direct role in thylakoid (Delta)pH-dependent protein transport. FEBS Lett 501 (2001) 65-68
    • (2001) FEBS Lett , vol.501 , pp. 65-68
    • Mori, H.1    Summer, E.J.2    Cline, K.3
  • 88
    • 0035964205 scopus 로고    scopus 로고
    • An essential role of a TatC homologue of a DeltapH-dependent protein transporter in thylakoid membrane formation during chloroplast development in Arabidopsis thaliana
    • Motohashi R., Nagata N., Ito T., Takahashi S., Hobo T., Yoshida S., and Shinozaki K. An essential role of a TatC homologue of a DeltapH-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
  • 90
    • 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., and Robinson C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J Biol Chem 276 (2001) 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
  • 91
    • 0346655242 scopus 로고    scopus 로고
    • Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway
    • DeLisa M.P., Lee P., Palmer T., and Georgiou G. Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. J Bacteriol 186 (2004) 366-373
    • (2004) J Bacteriol , vol.186 , pp. 366-373
    • DeLisa, M.P.1    Lee, P.2    Palmer, T.3    Georgiou, G.4
  • 92
    • 0242290351 scopus 로고    scopus 로고
    • Requirement of a Tha4-conserved transmembrane glutamate in thylakoid Tat translocase assembly revealed by biochemical complementation
    • Dabney-Smith C., Mori H., and Cline K. Requirement of a Tha4-conserved transmembrane glutamate in thylakoid Tat translocase assembly revealed by biochemical complementation. J Biol Chem 278 (2003) 43027-43033
    • (2003) J Biol Chem , vol.278 , pp. 43027-43033
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 93
    • 0036837744 scopus 로고    scopus 로고
    • Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation
    • Lee P.A., Buchanan G., Stanley N.R., Berks B.C., and Palmer T. Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation. J Bacteriol 184 (2002) 5871-5879
    • (2002) J Bacteriol , vol.184 , pp. 5871-5879
    • Lee, P.A.1    Buchanan, G.2    Stanley, N.R.3    Berks, B.C.4    Palmer, T.5
  • 94
    • 33646837543 scopus 로고    scopus 로고
    • Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
    • Dabney-Smith C., Mori H., and Cline K. Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J Biol Chem 281 (2006) 5476-5483
    • (2006) J Biol Chem , vol.281 , pp. 5476-5483
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 95
    • 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., and Cline K. A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase. J Cell Biol 157 (2002) 205-210
    • (2002) J Cell Biol , vol.157 , pp. 205-210
    • Mori, H.1    Cline, K.2
  • 96
    • 29444443773 scopus 로고    scopus 로고
    • Unassisted membrane insertion as the initial step in DeltapH/Tat-dependent protein transport
    • Hou B., Frielingsdorf S., and Klosgen R.B. Unassisted membrane insertion as the initial step in DeltapH/Tat-dependent protein transport. J Mol Biol 355 (2006) 957-967
    • (2006) J Mol Biol , vol.355 , pp. 957-967
    • Hou, B.1    Frielingsdorf, S.2    Klosgen, R.B.3
  • 97
    • 14644439237 scopus 로고    scopus 로고
    • Characterisation of Tat protein transport complexes carrying inactivating mutations
    • McDevitt C.A., Hicks M.G., Palmer T., and Berks B.C. Characterisation of Tat protein transport complexes carrying inactivating mutations. Biochem Biophys Res Commun 329 (2005) 693-698
    • (2005) Biochem Biophys Res Commun , vol.329 , pp. 693-698
    • McDevitt, C.A.1    Hicks, M.G.2    Palmer, T.3    Berks, B.C.4
  • 98
    • 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., and Cline K. Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site. J Biol Chem 281 (2006) 6130-6135
    • (2006) J Biol Chem , vol.281 , pp. 6130-6135
    • Gerard, F.1    Cline, K.2
  • 99
    • 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., and Muller M. 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    Muller, M.7
  • 100
    • 0033575188 scopus 로고    scopus 로고
    • Sec-dependent pathway and DeltapH-dependent pathway do not share a common translocation pore in thylakoidal protein transport
    • Asai T., Shinoda Y., Nohara T., Yoshihisa T., and Endo T. Sec-dependent pathway and DeltapH-dependent pathway do not share a common translocation pore in thylakoidal protein transport. J Biol Chem 274 (1999) 20075-20078
    • (1999) J Biol Chem , vol.274 , pp. 20075-20078
    • Asai, T.1    Shinoda, Y.2    Nohara, T.3    Yoshihisa, T.4    Endo, T.5
  • 101
    • 27544470676 scopus 로고    scopus 로고
    • Large-scale translocation reversal within the thylakoid Tat system in vivo
    • Di Cola A., and Robinson C. Large-scale translocation reversal within the thylakoid Tat system in vivo. J Cell Biol 171 (2005) 281-289
    • (2005) J Cell Biol , vol.171 , pp. 281-289
    • Di Cola, A.1    Robinson, C.2
  • 102
    • 0032512709 scopus 로고    scopus 로고
    • Evidence for a loop mechanism of protein transport by the thylakoid Delta pH pathway
    • Fincher V., McCaffery M., and Cline K. Evidence for a loop mechanism of protein transport by the thylakoid Delta pH pathway. FEBS Lett 423 (1998) 66-70
    • (1998) FEBS Lett , vol.423 , pp. 66-70
    • Fincher, V.1    McCaffery, M.2    Cline, K.3
  • 103
    • 0242444212 scopus 로고    scopus 로고
    • Two distinct translocation intermediates can be distinguished during protein transport by the TAT (Deltaph) pathway across the thylakoid membrane
    • Berghofer J., and Klosgen R.B. Two distinct translocation intermediates can be distinguished during protein transport by the TAT (Deltaph) pathway across the thylakoid membrane. FEBS Lett 460 (1999) 328-332
    • (1999) FEBS Lett , vol.460 , pp. 328-332
    • Berghofer, J.1    Klosgen, R.B.2
  • 104
    • 0033231926 scopus 로고    scopus 로고
    • How to get a folded protein across a membrane
    • Teter S.A., and Klionsky D.J. How to get a folded protein across a membrane. Trends Cell Biol 9 (1999) 428-431
    • (1999) Trends Cell Biol , vol.9 , pp. 428-431
    • Teter, S.A.1    Klionsky, D.J.2
  • 105
    • 0037274388 scopus 로고    scopus 로고
    • An alternative model of the twin arginine translocation system
    • Bruser T., and Sanders C. An alternative model of the twin arginine translocation system. Microbiol Res 158 (2003) 7-17
    • (2003) Microbiol Res , vol.158 , pp. 7-17
    • Bruser, T.1    Sanders, C.2
  • 106
    • 18844442890 scopus 로고    scopus 로고
    • The Tat pathway in bacteria and chloroplasts (review)
    • Muller M., and Klosgen R.B. The Tat pathway in bacteria and chloroplasts (review). Mol Membr Biol 22 (2005) 113-121
    • (2005) Mol Membr Biol , vol.22 , pp. 113-121
    • Muller, M.1    Klosgen, R.B.2
  • 107
    • 33745989572 scopus 로고    scopus 로고
    • Affinity of TATCd for TATAd elucidates its receptor function in the Bacillus subtilis tat translocase system
    • Schreiber S., Stengel R., Westermann M., Volkmer-Engert R., Pop O.I., and Muller J.P. Affinity of TATCd for TATAd elucidates its receptor function in the Bacillus subtilis tat translocase system. J Biol Chem 281 (2006) 19977-19984
    • (2006) J Biol Chem , vol.281 , pp. 19977-19984
    • Schreiber, S.1    Stengel, R.2    Westermann, M.3    Volkmer-Engert, R.4    Pop, O.I.5    Muller, J.P.6
  • 109
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi A., Sandri L., and Giangaspero A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 110
    • 1642523788 scopus 로고    scopus 로고
    • Dual topology of the Escherichia coli TatA protein
    • Gouffi K., Gerard F., Santini C.L., and Wu L.F. Dual topology of the Escherichia coli TatA protein. J Biol Chem 279 (2004) 11608-11615
    • (2004) J Biol Chem , vol.279 , pp. 11608-11615
    • Gouffi, K.1    Gerard, F.2    Santini, C.L.3    Wu, L.F.4
  • 111
    • 33747192339 scopus 로고    scopus 로고
    • Altered rates of protein transport in Arabidopsis mutants deficient in chloroplast membrane unsaturation
    • Ma X., and Browse J. Altered rates of protein transport in Arabidopsis mutants deficient in chloroplast membrane unsaturation. Phytochemistry 67 (2006) 1629-1636
    • (2006) Phytochemistry , vol.67 , pp. 1629-1636
    • Ma, X.1    Browse, J.2
  • 112
    • 0033407138 scopus 로고    scopus 로고
    • Requirement for phospholipids of the translocation of the trimethylamine N-oxide reductase through the Tat pathway in Escherichia coli
    • Mikhaleva N.I., Santini C.L., Giordano G., Nesmeyanova M.A., and Wu L.F. Requirement for phospholipids of the translocation of the trimethylamine N-oxide reductase through the Tat pathway in Escherichia coli. FEBS Lett 463 (1999) 331-335
    • (1999) FEBS Lett , vol.463 , pp. 331-335
    • Mikhaleva, N.I.1    Santini, C.L.2    Giordano, G.3    Nesmeyanova, M.A.4    Wu, L.F.5


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