메뉴 건너뛰기




Volumn 71, Issue 4, 2012, Pages 656-668

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid

Author keywords

chloroplast; cpTat; Pisum sativum; protein transport; substrate binding; thylakoid; VIPP1

Indexed keywords

CHLOROPLAST; CPTAT; PISUM SATIVUM; PROTEIN TRANSPORT; SUBSTRATE-BINDING; THYLAKOIDS; VIPP1;

EID: 84864601625     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2012.05020.x     Document Type: Article
Times cited : (42)

References (65)
  • 1
    • 0030896924 scopus 로고    scopus 로고
    • Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking
    • Akita, M., Nielsen, E., and, Keegstra, K., (1997) Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking. J. Cell Biol. 136, 983-994.
    • (1997) J. Cell Biol. , vol.136 , pp. 983-994
    • Akita, M.1    Nielsen, E.2    Keegstra, K.3
  • 3
    • 0037462475 scopus 로고    scopus 로고
    • Energetics of protein transport across biological membranes: A study of the thylakoid ΔpH-dependent/cpTat pathway
    • Alder, N., and, Theg, S., (2003) Energetics of protein transport across biological membranes: a study of the thylakoid ΔpH-dependent/cpTat pathway. Cell, 112, 231-242.
    • (2003) Cell , vol.112 , pp. 231-242
    • Alder, N.1    Theg, S.2
  • 4
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    • Arnon, D., (1949) Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol. 24, 1-14.
    • (1949) Plant Physiol. , vol.24 , pp. 1-14
    • Arnon, D.1
  • 6
    • 70350180744 scopus 로고    scopus 로고
    • Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI
    • Bageshwar, U., Whitaker, N., Liang, F., and, Musser, S., (2009) Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI. Mol. Microbiol. 74, 209-226.
    • (2009) Mol. Microbiol. , vol.74 , pp. 209-226
    • Bageshwar, U.1    Whitaker, N.2    Liang, F.3    Musser, S.4
  • 7
    • 44049090400 scopus 로고    scopus 로고
    • The chloroplast Tat pathway transports substrates in the dark
    • Braun, N., and, Theg, S., (2008) The chloroplast Tat pathway transports substrates in the dark. J. Biol. Chem. 283, 8822-8828.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8822-8828
    • Braun, N.1    Theg, S.2
  • 8
    • 34548756762 scopus 로고    scopus 로고
    • The chloroplast Tat pathway utilizes the transmembrane electric potential as an energy source
    • Braun, N., Davis, A., and, Theg, S., (2007) The chloroplast Tat pathway utilizes the transmembrane electric potential as an energy source. Biophys. J. 93, 1993-1998.
    • (2007) Biophys. J. , vol.93 , pp. 1993-1998
    • Braun, N.1    Davis, A.2    Theg, S.3
  • 11
    • 0030918441 scopus 로고    scopus 로고
    • A folded protein can be transported across the chloroplast envelope and thylakoid membranes
    • Clark, S., and, Theg, S., (1997) A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol. Biol. Cell 8, 923-934.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 923-934
    • Clark, S.1    Theg, S.2
  • 12
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • Cline, K., and, Mori, H., (2001) Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J. Cell Biol. 154, 719-729.
    • (2001) J. Cell Biol. , vol.154 , pp. 719-729
    • Cline, K.1    Mori, H.2
  • 13
    • 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., and, Theg, S., (1992) 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, 2688-2696.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.2    Theg, S.3
  • 14
    • 0027494820 scopus 로고
    • Multiple pathways for protein transport into or across the thylakoid membrane
    • Cline, K., Henry, R., Li, C., and, Yuan, J., (1993) Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J. 12, 4105-4114.
    • (1993) EMBO J. , vol.12 , pp. 4105-4114
    • Cline, K.1    Henry, R.2    Li, C.3    Yuan, J.4
  • 15
    • 0028945041 scopus 로고
    • A monomeric, tightly folded stromal intermediate on the pH-dependent thylakoidal protein transport pathway
    • Creighton, A., Hulford, A., Mant, A., Robinson, D., and, Robinson, C., (1995) A monomeric, tightly folded stromal intermediate on the pH-dependent thylakoidal protein transport pathway. J. Biol. Chem. 270, 1663-1669.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1663-1669
    • Creighton, A.1    Hulford, A.2    Mant, A.3    Robinson, D.4    Robinson, C.5
  • 16
    • 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., (2006) Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J. Biol. Chem. 281, 5476-5483.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5476-5483
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 17
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa, M., Tullman, D., and, Georgiou, G., (2003) Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl Acad. Sci. USA, 100, 6115-6120.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6115-6120
    • Delisa, M.1    Tullman, D.2    Georgiou, G.3
  • 18
    • 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., (2004) Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. J. Bacteriol. 186, 366-373.
    • (2004) J. Bacteriol. , vol.186 , pp. 366-373
    • Delisa, M.P.1    Lee, P.2    Palmer, T.3    Georgiou, G.4
  • 19
    • 57749090396 scopus 로고    scopus 로고
    • A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane
    • Frielingsdorf, S., Jakob, M., and, Klösgen, R., (2008) A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane. J. Biol. Chem. 283, 33838-33845.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33838-33845
    • Frielingsdorf, S.1    Jakob, M.2    Klösgen, R.3
  • 20
    • 75649138339 scopus 로고    scopus 로고
    • Phosphorylation of photosystem II controls functional macroscopic folding of photosynthetic membranes in Arabidopsis
    • Fristedt, R., Willig, A., Granath, P., Crèvecoeur, M., Rochaix, J., and, Vener, A., (2009) Phosphorylation of photosystem II controls functional macroscopic folding of photosynthetic membranes in Arabidopsis. Plant Cell, 21, 3950-3964.
    • (2009) Plant Cell , vol.21 , pp. 3950-3964
    • Fristedt, R.1    Willig, A.2    Granath, P.3    Crèvecoeur, M.4    Rochaix, J.5    Vener, A.6
  • 21
    • 73949092282 scopus 로고    scopus 로고
    • The vesicle-inducing protein 1 from Synechocystis sp. PCC 6803 organizes into diverse higher-ordered ring structures
    • Fuhrmann, E., Bultema, J., Kahmann, U., Rupprecht, E., Boekema, E., and, Schneider, D., (2009a) The vesicle-inducing protein 1 from Synechocystis sp. PCC 6803 organizes into diverse higher-ordered ring structures. Mol. Biol. Cell 20, 4620-4628.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4620-4628
    • Fuhrmann, E.1    Bultema, J.2    Kahmann, U.3    Rupprecht, E.4    Boekema, E.5    Schneider, D.6
  • 22
    • 60249102598 scopus 로고    scopus 로고
    • Thylakoid membrane reduction affects the photosystem stoichiometry in the cyanobacterium Synechocystis sp. PCC 6803
    • Fuhrmann, E., Gathmann, S., Rupprecht, E., Golecki, J., and, Schneider, D., (2009b) Thylakoid membrane reduction affects the photosystem stoichiometry in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiol. 149, 735-744.
    • (2009) Plant Physiol. , vol.149 , pp. 735-744
    • Fuhrmann, E.1    Gathmann, S.2    Rupprecht, E.3    Golecki, J.4    Schneider, D.5
  • 23
    • 59349113257 scopus 로고    scopus 로고
    • Depletion of Vipp1 in Synechocystis sp. PCC 6803 affects photosynthetic activity before the loss of thylakoid membranes
    • Gao, H., and, Xu, X., (2009) Depletion of Vipp1 in Synechocystis sp. PCC 6803 affects photosynthetic activity before the loss of thylakoid membranes. FEMS Microbiol. Lett. 292, 63-70.
    • (2009) FEMS Microbiol. Lett. , vol.292 , pp. 63-70
    • Gao, H.1    Xu, X.2
  • 24
    • 34147125271 scopus 로고    scopus 로고
    • DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone
    • Graubner, W., Schierhorn, A., and, Brüser, T., (2007) DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone. J. Biol. Chem. 282, 7116-7124.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7116-7124
    • Graubner, W.1    Schierhorn, A.2    Brüser, T.3
  • 26
    • 29444443773 scopus 로고    scopus 로고
    • Unassisted membrane insertion as the initial step in ΔpH/Tat- dependent protein transport
    • Hou, B., Frielingsdorf, S., and, Klösgen, R., (2006) Unassisted membrane insertion as the initial step in ΔpH/Tat-dependent protein transport. J. Mol. Biol. 355, 957-967.
    • (2006) J. Mol. Biol. , vol.355 , pp. 957-967
    • Hou, B.1    Frielingsdorf, S.2    Klösgen, R.3
  • 27
    • 0013829310 scopus 로고
    • Washing bacteria by centrifugation through a water-immiscible layer of silicones
    • Hurwitz, C., Braun, C., and, Peabody, R., (1965) Washing bacteria by centrifugation through a water-immiscible layer of silicones. J. Bacteriol. 90, 1692-1695.
    • (1965) J. Bacteriol. , vol.90 , pp. 1692-1695
    • Hurwitz, C.1    Braun, C.2    Peabody, R.3
  • 28
    • 58549086935 scopus 로고    scopus 로고
    • Tat subunit stoichiometry in Arabidopsis thaliana challenges the proposed function of TatA as the translocation pore
    • Jakob, M., Kaiser, S., Gutensohn, M., Hanner, P., and, Klösgen, R., (2009) Tat subunit stoichiometry in Arabidopsis thaliana challenges the proposed function of TatA as the translocation pore. Biochim. Biophys. Acta 1793, 388-394.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 388-394
    • Jakob, M.1    Kaiser, S.2    Gutensohn, M.3    Hanner, P.4    Klösgen, R.5
  • 29
    • 67650532151 scopus 로고    scopus 로고
    • Interaction of actin and the chloroplast protein import apparatus
    • Jouhet, J., and, Gray, J., (2009) Interaction of actin and the chloroplast protein import apparatus. J. Biol. Chem. 284, 19132-19141.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19132-19141
    • Jouhet, J.1    Gray, J.2
  • 30
    • 13144269970 scopus 로고
    • Electrogenic reactions and proton pumping in green plant photosynthesis
    • Junge, W., (1982) Electrogenic reactions and proton pumping in green plant photosynthesis. Curr. Topics Membr. Transport 16, 431-464.
    • (1982) Curr. Topics Membr. Transport , vol.16 , pp. 431-464
    • Junge, W.1
  • 31
    • 0014247117 scopus 로고
    • On the ion transport system of photosynthesis - Investigations on a molecular level
    • Junge, W., and, Witt, H., (1968) On the ion transport system of photosynthesis-investigations on a molecular level. Z. Naturforsch. B. 23, 244-254.
    • (1968) Z. Naturforsch. B. , vol.23 , pp. 244-254
    • Junge, W.1    Witt, H.2
  • 32
    • 43049166553 scopus 로고    scopus 로고
    • Protein diffusion and macromolecular crowding in thylakoid membranes
    • Kirchhoff, H., Haferkamp, S., Allen, J., Epstein, D., and, Mullineaux, C., (2008) Protein diffusion and macromolecular crowding in thylakoid membranes. Plant Physiol. 146, 1571-1578.
    • (2008) Plant Physiol. , vol.146 , pp. 1571-1578
    • Kirchhoff, H.1    Haferkamp, S.2    Allen, J.3    Epstein, D.4    Mullineaux, C.5
  • 33
    • 0027522364 scopus 로고
    • Expression of the pspA gene stimulates efficient protein export in Escherichia coli
    • Kleerebezem, M., and, Tommassen, J., (1993) Expression of the pspA gene stimulates efficient protein export in Escherichia coli. Mol. Microbiol. 7, 947-956.
    • (1993) Mol. Microbiol. , vol.7 , pp. 947-956
    • Kleerebezem, M.1    Tommassen, J.2
  • 34
    • 0030028862 scopus 로고    scopus 로고
    • Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions
    • Kleerebezem, M., Crielaard, W., and, Tommassen, J., (1996) Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions. EMBO J. 15, 162-171.
    • (1996) EMBO J. , vol.15 , pp. 162-171
    • Kleerebezem, M.1    Crielaard, W.2    Tommassen, J.3
  • 35
    • 34548704307 scopus 로고    scopus 로고
    • Escherichia coli phage-shock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes
    • Kobayashi, R., Suzuki, T., and, Yoshida, M., (2007) Escherichia coli phage-shock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes. Mol. Microbiol. 66, 100-109.
    • (2007) Mol. Microbiol. , vol.66 , pp. 100-109
    • Kobayashi, R.1    Suzuki, T.2    Yoshida, M.3
  • 37
    • 0001336374 scopus 로고    scopus 로고
    • Identification of a role for an azide-sensitive factor in the thylakoid transport of the 17-kilodalton subunit of the photosynthetic oxygen-evolving complex
    • Leheny, E., Teter, S., and, Theg, S., (1998) Identification of a role for an azide-sensitive factor in the thylakoid transport of the 17-kilodalton subunit of the photosynthetic oxygen-evolving complex. Plant Physiol. 116, 805-814.
    • (1998) Plant Physiol. , vol.116 , pp. 805-814
    • Leheny, E.1    Teter, S.2    Theg, S.3
  • 38
    • 78650244316 scopus 로고    scopus 로고
    • State transitions at the crossroad of thylakoid signalling pathways
    • Lemeille, S., and, Rochaix, J., (2010) State transitions at the crossroad of thylakoid signalling pathways. Photosynth. Res. 106, 33-46.
    • (2010) Photosynth. Res. , vol.106 , pp. 33-46
    • Lemeille, S.1    Rochaix, J.2
  • 39
    • 0028467779 scopus 로고
    • Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes
    • Li, H., Kaneko, Y., and, Keegstra, K., (1994) Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes. Plant Mol. Biol. 25, 619-632.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 619-632
    • Li, H.1    Kaneko, Y.2    Keegstra, K.3
  • 40
    • 33645365498 scopus 로고    scopus 로고
    • Coexpression of TorD enhances the transport of GFP via the Tat pathway
    • Li, S., Chang, B., and, Lin, S., (2006) Coexpression of TorD enhances the transport of GFP via the Tat pathway. J. Biotechnol. 122, 412-421.
    • (2006) J. Biotechnol. , vol.122 , pp. 412-421
    • Li, S.1    Chang, B.2    Lin, S.3
  • 41
    • 14844293494 scopus 로고    scopus 로고
    • J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with Vesicle-Inducing Protein in Plastids 1
    • Liu, C., Willmund, F., Whitelegge, J., Hawat, S., Knapp, B., Lodha, M., and, Schroda, M,. (2005) J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with Vesicle-Inducing Protein in Plastids 1. Mol. Biol. Cell. 16, 1165-1177.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1165-1177
    • Liu, C.1    Willmund, F.2    Whitelegge, J.3    Hawat, S.4    Knapp, B.5    Lodha, M.6    Schroda, M.7
  • 42
    • 79952115702 scopus 로고    scopus 로고
    • Protein targeting across and into chloroplast membranes
    • Lo, S., and, Theg, S., (2011) Protein targeting across and into chloroplast membranes. Methods Mol. Biol. 684, 139-157.
    • (2011) Methods Mol. Biol. , vol.684 , pp. 139-157
    • Lo, S.1    Theg, S.2
  • 43
    • 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., (2000) Precursors bind to specific sites on thylakoid membranes prior to transport on the delta pH protein translocation system. J. Biol. Chem. 275, 10016-10022.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10016-10022
    • Ma, X.1    Cline, K.2
  • 44
    • 77951978000 scopus 로고    scopus 로고
    • Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported
    • Ma, X., and, Cline, K., (2010) Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported. EMBO J. 29, 1477-1488.
    • (2010) EMBO J. , vol.29 , pp. 1477-1488
    • Ma, X.1    Cline, K.2
  • 45
    • 4043075625 scopus 로고    scopus 로고
    • In vivo transport of folded EGFP by the ΔpH/Tat-dependent pathway in chloroplasts of Arabidopsis thaliana
    • Marques, J., Scatted, M., House, G., Dudes, I., and, Klösgen, R., (2004) In vivo transport of folded EGFP by the ΔpH/Tat-dependent pathway in chloroplasts of Arabidopsis thaliana. J. Exp. Bot. 55, 1697-1706.
    • (2004) J. Exp. Bot. , vol.55 , pp. 1697-1706
    • Marques, J.1    Scatted, M.2    House, G.3    Dudes, I.4    Klösgen, R.5
  • 46
    • 0037092039 scopus 로고    scopus 로고
    • A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
    • Mori, H., and, Cline, K., (2002) A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase. J. Cell Biol. 157, 205-210.
    • (2002) J. Cell Biol. , vol.157 , pp. 205-210
    • Mori, H.1    Cline, K.2
  • 47
    • 0033549567 scopus 로고    scopus 로고
    • Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways
    • Mori, H., Summer, E., Ma, X., and, Cline, K., (1999) Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways. J. Cell Biol. 146, 45-56.
    • (1999) J. Cell Biol. , vol.146 , pp. 45-56
    • Mori, H.1    Summer, E.2    Ma, X.3    Cline, K.4
  • 48
    • 0035854799 scopus 로고    scopus 로고
    • Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport
    • Mori, H., Summer, E., and, Cline, K., (2001) Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport. FEBS Lett. 501, 65-68.
    • (2001) FEBS Lett. , vol.501 , pp. 65-68
    • Mori, H.1    Summer, E.2    Cline, K.3
  • 49
    • 0025781325 scopus 로고
    • A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane
    • Mould, R., and, Robinson, C., (1991) A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J. Biol. Chem. 266, 12189-12193.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12189-12193
    • Mould, R.1    Robinson, C.2
  • 50
    • 0026050854 scopus 로고
    • Transport of proteins into chloroplasts. Requirements for the efficient import of two lumenal oxygen-evolving complex proteins into isolated thylakoids
    • Mould, R., Shackleton, J., and, Robinson, C., (1991) Transport of proteins into chloroplasts. Requirements for the efficient import of two lumenal oxygen-evolving complex proteins into isolated thylakoids. J. Biol. Chem. 266, 17286-17289.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17286-17289
    • Mould, R.1    Shackleton, J.2    Robinson, C.3
  • 51
    • 0034031057 scopus 로고    scopus 로고
    • Characterization of the early steps of OE17 precursor transport by the thylakoid ΔpH/Tat machinery
    • Musser, S., and, Theg, S., (2000) Characterization of the early steps of OE17 precursor transport by the thylakoid ΔpH/Tat machinery. Eur. J. Biochem. 267, 2588-2598.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2588-2598
    • Musser, S.1    Theg, S.2
  • 52
    • 84859098116 scopus 로고    scopus 로고
    • Evidence for a role of VIPP1 in the structural organization of the photosynthetic apparatus in Chlamydomonas
    • Nordhues, A., Schöttler, M.A., Unger, A.K., et al. (2012) Evidence for a role of VIPP1 in the structural organization of the photosynthetic apparatus in Chlamydomonas. Plant Cell, 24, 637-659.
    • (2012) Plant Cell , vol.24 , pp. 637-659
    • Nordhues, A.1    Schöttler, M.A.2    Unger, A.K.3
  • 53
    • 33847396185 scopus 로고    scopus 로고
    • An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway
    • Pérez-Rodríguez, R., Fisher, A., Perlmutter, J., Hicks, M., Chanal, A., Santini, C., Wu, L., Palmer, T., and, DeLisa, M., (2007) An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway. J. Mol. Biol. 367, 715-730.
    • (2007) J. Mol. Biol. , vol.367 , pp. 715-730
    • Pérez-Rodríguez, R.1    Fisher, A.2    Perlmutter, J.3    Hicks, M.4    Chanal, A.5    Santini, C.6    Wu, L.7    Palmer, T.8    Delisa, M.9
  • 54
    • 79951480123 scopus 로고    scopus 로고
    • R Development Core Team. Vienna, Austria: R Foundation for Statistical Computing.
    • R Development Core Team (2010) R: A Language and Environment for Statistical Computing. Vienna, Austria: R Foundation for Statistical Computing.
    • (2010) R: A Language and Environment for Statistical Computing
  • 55
    • 0035723135 scopus 로고    scopus 로고
    • A portable, non-focusing optics spectrophotometer (NoFOSpec) for measurements of steady-state absorbance changes in intact plants
    • Sacksteder, C., Jacoby, M., and, Kramer, D., (2001) A portable, non-focusing optics spectrophotometer (NoFOSpec) for measurements of steady-state absorbance changes in intact plants. Photosynth. Res. 70, 231-240.
    • (2001) Photosynth. Res. , vol.70 , pp. 231-240
    • Sacksteder, C.1    Jacoby, M.2    Kramer, D.3
  • 56
    • 0015530426 scopus 로고
    • Determination of pH in chloroplasts. 2. Fluorescent amines as a probe for the determination of pH in chloroplasts
    • Schuldiner, S., Rotenberg, H., and, Avon, M., (1972) Determination of pH in chloroplasts. 2. Fluorescent amines as a probe for the determination of pH in chloroplasts. Eur. J. Biochem. 25, 64-70.
    • (1972) Eur. J. Biochem. , vol.25 , pp. 64-70
    • Schuldiner, S.1    Rotenberg, H.2    Avon, M.3
  • 57
    • 33144481331 scopus 로고    scopus 로고
    • Membrane binding of twin arginine proportions as an early step in translocation
    • Shanmugham, A., Wong Fong Sang, H., Bolin, Y., and, Lilly, H., (2006) Membrane binding of twin arginine proportions as an early step in translocation. Biochemistry, 45, 2243-2249.
    • (2006) Biochemistry , vol.45 , pp. 2243-2249
    • Shanmugham, A.1    Wong Fong Sang, H.2    Bolin, Y.3    Lilly, H.4
  • 58
    • 0032539535 scopus 로고    scopus 로고
    • Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation
    • Teter, S., and, Theg, S., (1998) Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation. Proc. Natl Acad. Sci. USA, 95, 1590-1594.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1590-1594
    • Teter, S.1    Theg, S.2
  • 59
    • 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., Daniel, R., Errington, J., and, 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.1    Daniel, R.2    Errington, J.3    Robinson, C.4
  • 60
    • 71749083323 scopus 로고    scopus 로고
    • Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network
    • Vladimirou, E., Li, M., Aldridge, C., Frigerio, L., Kirkilionis, M., and, Robinson, C., (2009) Diffusion of a membrane protein, Tat subunit Hcf106, is highly restricted within the chloroplast thylakoid network. FEBS Lett. 583, 3690-3696.
    • (2009) FEBS Lett. , vol.583 , pp. 3690-3696
    • Vladimirou, E.1    Li, M.2    Aldridge, C.3    Frigerio, L.4    Kirkilionis, M.5    Robinson, C.6
  • 61
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker, R., and, Barkan, A., (1995) Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J. 14, 3905-3914.
    • (1995) EMBO J. , vol.14 , pp. 3905-3914
    • Voelker, R.1    Barkan, A.2
  • 63
    • 47049123612 scopus 로고    scopus 로고
    • Characterization of the Streptomyces lividans PspA response
    • Vrancken, K., Van Mellaert, L., and, Anné, J., (2008) Characterization of the Streptomyces lividans PspA response. J. Bacteriol. 190, 3475-3481.
    • (2008) J. Bacteriol. , vol.190 , pp. 3475-3481
    • Vrancken, K.1    Van Mellaert, L.2    Anné, J.3
  • 64
    • 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., Roy, L., Coleman, E., Voelker, R., and, Barkan, A., (1999) The maize tha4 gene functions in Sec-independent protein transport in chloroplasts and is related to hcf106, tatA, and tatB. J. Cell Biol. 147, 267-276.
    • (1999) J. Cell Biol. , vol.147 , pp. 267-276
    • Walker, M.1    Roy, L.2    Coleman, E.3    Voelker, R.4    Barkan, A.5
  • 65
    • 0035957413 scopus 로고    scopus 로고
    • Vipp1 deletion mutant of Synechocystis: A connection between bacterial phage shock and thylakoid biogenesis?
    • Westphal, S., Heins, L., Soll, J., and, Vothknecht, U., (2001) Vipp1 deletion mutant of Synechocystis: a connection between bacterial phage shock and thylakoid biogenesis? Proc. Natl Acad. Sci. USA, 98, 4243-4248.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4243-4248
    • Westphal, S.1    Heins, L.2    Soll, J.3    Vothknecht, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.