메뉴 건너뛰기




Volumn 38, Issue 1-2, 1998, Pages 209-221

Multiple pathways for the targeting of thylakoid proteins in chloroplasts

Author keywords

Chloroplasts; Membrane proteins; Protein transport; Signal peptides; Thylakoid

Indexed keywords

CARRIER PROTEIN; CELL NUCLEUS; CELL ORGANELLE; CHLOROPLAST; PHOTOSYNTHESIS; PROTEIN TARGETING; THYLAKOID;

EID: 0032169929     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-94-011-5298-3_11     Document Type: Article
Times cited : (55)

References (84)
  • 1
    • 0242455249 scopus 로고
    • Nucleotide sequence of the gene for preapocytochrome f in the spinach plastid genome
    • Alt J, Herrmann RG: Nucleotide sequence of the gene for preapocytochrome f in the spinach plastid genome. Curr Genet 8: 551-557 (1984).
    • (1984) Curr Genet , vol.8 , pp. 551-557
    • Alt, J.1    Herrmann, R.G.2
  • 2
    • 0027729984 scopus 로고
    • Components of the protein translocation machinery in the thermophilic cyanobacterium Phormidium laminosum
    • Barbrook A, Packer JC, Howe CJ: Components of the protein translocation machinery in the thermophilic cyanobacterium Phormidium laminosum. Biochem. Biophys, Res Comm 197: 874-877 (1993).
    • (1993) Biochem. Biophys, Res Comm , vol.197 , pp. 874-877
    • Barbrook, A.1    Packer, J.C.2    Howe, C.J.3
  • 3
    • 0026316318 scopus 로고
    • Transport of proteins into chloroplasts: Delineation of envelope transit and thylakoid transfer signals within the presequences of three imported thylakoid lumen proteins
    • Bassham DC, Bartling D, Mould RM, Dunbar B, Weisbeek P, Herrmann RG, Robinson C: Transport of proteins into chloroplasts: delineation of envelope transit and thylakoid transfer signals within the presequences of three imported thylakoid lumen proteins. J Biol Chem 266: 23606-23610 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 23606-23610
    • Bassham, D.C.1    Bartling, D.2    Mould, R.M.3    Dunbar, B.4    Weisbeek, P.5    Herrmann, R.G.6    Robinson, C.7
  • 4
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks BC: A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22: 393-404 (1996).
    • (1996) Mol Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 5
    • 0030976930 scopus 로고    scopus 로고
    • Pathway specificity for a ΔpH-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, Robinson C: Pathway specificity for a ΔpH-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: 3851-3858 (1997).
    • (1997) EMBO J , vol.16 , pp. 3851-3858
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 6
    • 0030978698 scopus 로고    scopus 로고
    • Unusual characteristics of aminoterminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides
    • Brink S, Bogsch E, Mant A, Robinson C: Unusual characteristics of aminoterminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides. Eur J Biochem 245: 340-348 (1997).
    • (1997) Eur J Biochem , vol.245 , pp. 340-348
    • Brink, S.1    Bogsch, E.2    Mant, A.3    Robinson, C.4
  • 7
    • 0025507540 scopus 로고
    • Copper-induced expression, cloning and regulatory studies of the plastocyanin gene from the cyanobacterium Synechocystis sp. PCC 6803
    • Briggs LM, Pecoraro VL, McIntosh L: Copper-induced expression, cloning and regulatory studies of the plastocyanin gene from the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 15: 633-642 (1990).
    • (1990) Plant Mol Biol , vol.15 , pp. 633-642
    • Briggs, L.M.1    Pecoraro, V.L.2    McIntosh, L.3
  • 8
    • 0009632328 scopus 로고
    • The 20 kDa apoprotein of the CP24 complex of photosystem II: An alternative model to study import and intra-organellar routing of nuclear-encoded thylakoid proteins
    • Cai D, Herrmann RG, Klösgen RB: The 20 kDa apoprotein of the CP24 complex of photosystem II: an alternative model to study import and intra-organellar routing of nuclear-encoded thylakoid proteins. Plant J 3: 383-392 (1993).
    • (1993) Plant J , vol.3 , pp. 383-392
    • Cai, D.1    Herrmann, R.G.2    Klösgen, R.B.3
  • 9
    • 0031975202 scopus 로고    scopus 로고
    • Characterisation of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana
    • Chaal B, Howe CJ: Characterisation of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana. J Biol Chem 273: 689-692 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 689-692
    • Chaal, B.1    Howe, C.J.2
  • 10
    • 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
    • Chaddock AM, Mant A, Karnauchov I, Brink S, Herrmann RG, Klösgen RB, Robinson C: 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: 2715-2722 (1995).
    • (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
  • 11
    • 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, Klösgen RB, Herrmann RG: 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: 13869-13876 (1989).
    • (1989) J Biol Chem , vol.268 , pp. 13869-13876
    • Clausmeyer, S.1    Klösgen, R.B.2    Herrmann, R.G.3
  • 12
    • 0009649754 scopus 로고
    • Insertion of the precursor of the light-harvesting chlorophyll a/b protein into the thylakoids requires the presence of a developmentally regulated stromal factor
    • Chitnis PR, Nechushtai R, Thornber JP: Insertion of the precursor of the light-harvesting chlorophyll a/b protein into the thylakoids requires the presence of a developmentally regulated stromal factor. Plant Mol Biol 10: 3-11 (1987).
    • (1987) Plant Mol Biol , vol.10 , pp. 3-11
    • Chitnis, P.R.1    Nechushtai, R.2    Thornber, J.P.3
  • 13
    • 0030918441 scopus 로고    scopus 로고
    • A folded protein can be transported across the chloroplast envelope and thylakoid membranes
    • Clark SA, Theg SM: A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol Biol Cell 8: 923-934 (1997).
    • (1997) Mol Biol Cell , vol.8 , pp. 923-934
    • Clark, S.A.1    Theg, S.M.2
  • 14
    • 0022851237 scopus 로고
    • Import of proteins into chloroplasts: Membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates
    • Cline K: Import of proteins into chloroplasts: membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates. J Biol Chem 261: 14804-14810 (1986).
    • (1986) J Biol Chem , vol.261 , pp. 14804-14810
    • Cline, K.1
  • 15
    • 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 WF, Theg SM: 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).
    • (1992) J Biol Chem , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 16
    • 0027494820 scopus 로고
    • Multiple pathways for protein transport into or across the thylakoid membrane
    • Cline K, Henry R, Li C, Yuan J: Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J 12: 1405-4114 (1993).
    • (1993) EMBO J , vol.12 , pp. 1405-4114
    • Cline, K.1    Henry, R.2    Li, C.3    Yuan, J.4
  • 18
    • 0030590843 scopus 로고    scopus 로고
    • Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle
    • de Gier J-WL, Mansournia P, Valent QA, Phillips GJ, Luirink J, von Heijne G: Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle. FEBS Lett 399: 307-309 (1997).
    • (1997) FEBS Lett , vol.399 , pp. 307-309
    • De Gier, J.-W.L.1    Mansournia, P.2    Valent, Q.A.3    Phillips, G.J.4    Luirink, J.5    Von Heijne, G.6
  • 19
    • 0027476967 scopus 로고
    • SecY, an integral subunit of the bacterial preprotein translocase, is encoded by a plastid genome
    • Flachmann R, Michalowski CB, Löffelhardt W, Bohnert HJ: SecY, an integral subunit of the bacterial preprotein translocase, is encoded by a plastid genome. J Biol Chem 268: 7514-7519 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 7514-7519
    • Flachmann, R.1    Michalowski, C.B.2    Löffelhardt, W.3    Bohnert, H.J.4
  • 20
    • 0027377619 scopus 로고
    • Chloroplasts contain a homolog of the 54 kD subunit of the signal recognition particle
    • Franklin AE, Hoffman NE: Chloroplasts contain a homolog of the 54 kD subunit of the signal recognition particle. J Biol Chem 268: 22175-22180 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 22175-22180
    • Franklin, A.E.1    Hoffman, N.E.2
  • 22
    • 0001610085 scopus 로고
    • Thylakoid processing protease is required for complete maturation of the lumen protein plastocyanin
    • Hageman J, Robinson C, Smeekens S, Weisbeek PA: thylakoid processing protease is required for complete maturation of the lumen protein plastocyanin. Nature 324: 567-569 (1986).
    • (1986) Nature , vol.324 , pp. 567-569
    • Hageman, J.1    Robinson, C.2    Smeekens, S.3    Weisbeek, P.A.4
  • 23
    • 0000303677 scopus 로고
    • Protein import into and sorting inside the chloroplast are independent processes
    • Hageman J, Baecke C, Ebskamp M, Pilon R, Smeekens S, Weisbeek P: Protein import into and sorting inside the chloroplast are independent processes. Plant Cell 2: 479-494 (1990).
    • (1990) Plant Cell , vol.2 , pp. 479-494
    • Hageman, J.1    Baecke, C.2    Ebskamp, M.3    Pilon, R.4    Smeekens, S.5    Weisbeek, P.6
  • 24
    • 0024852098 scopus 로고
    • The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical
    • Halpin C, Elderfield PD, James HE, Zimmermann R, Dunbar B, Robinson C: The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical. EMBO J 8: 3917-3921 (1989).
    • (1989) EMBO J , vol.8 , pp. 3917-3921
    • Halpin, C.1    Elderfield, P.D.2    James, H.E.3    Zimmermann, R.4    Dunbar, B.5    Robinson, C.6
  • 25
    • 0024462106 scopus 로고
    • The transit peptide of a chloroplast thylakoid membrane protein is functionally equivalent to a stromal-targeting sequence
    • Hand JM, Szabo LJ, Vasconcelos AC, Cashmore AR: The transit peptide of a chloroplast thylakoid membrane protein is functionally equivalent to a stromal-targeting sequence. EMBO J 8: 3195-3206 (1989).
    • (1989) EMBO J , vol.8 , pp. 3195-3206
    • Hand, J.M.1    Szabo, L.J.2    Vasconcelos, A.C.3    Cashmore, A.R.4
  • 26
    • 0001129473 scopus 로고
    • Chloroplast ATP synthase of spinach contains nine nonidentical subunit species, six of which are encoded by plastid chromosomes in two operons in a phylogenetically conserved arrangement
    • Hennig J, Herrmann RG: Chloroplast ATP synthase of spinach contains nine nonidentical subunit species, six of which are encoded by plastid chromosomes in two operons in a phylogenetically conserved arrangement. Mol Gen Genet 203: 117-128 (1986).
    • (1986) Mol Gen Genet , vol.203 , pp. 117-128
    • Hennig, J.1    Herrmann, R.G.2
  • 27
    • 0028290813 scopus 로고
    • Differences between lumen targeting domains of chloroplast transit peptides determine pathway specificity for thylakoid transport
    • Henry R, Kapazoglou A, McCaffery M, Cline K: Differences between lumen targeting domains of chloroplast transit peptides determine pathway specificity for thylakoid transport. J Biol Chem 269: 10189-10192 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 10189-10192
    • Henry, R.1    Kapazoglou, A.2    McCaffery, M.3    Cline, K.4
  • 28
    • 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, 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: 823-832 (1997).
    • (1997) J Cell Biol , vol.136 , pp. 823-832
    • Henry, R.1    Carrigan, M.2    McCaffrey, M.3    Ma, X.4    Cline, K.5
  • 29
    • 0027156160 scopus 로고
    • The nuclear-encoded polypeptide CFoII from spinach is a real, ninth subunit of chloroplast ATP synthase
    • Herrmann RG, Steppuhn J, Herrmann GS, Nelson N: The nuclear-encoded polypeptide CFoII from spinach is a real, ninth subunit of chloroplast ATP synthase. FEBS Lett 326: 192-198 (1993).
    • (1993) FEBS Lett , vol.326 , pp. 192-198
    • Herrmann, R.G.1    Steppuhn, J.2    Herrmann, G.S.3    Nelson, N.4
  • 31
    • 0028430193 scopus 로고
    • Evidence for a stromal GTP requirement for the integration of a chlorophyll a/b binding polypeptide into thylakoid membranes
    • Hoffman NE, Franklin AE: Evidence for a stromal GTP requirement for the integration of a chlorophyll a/b binding polypeptide into thylakoid membranes. Plant Physiol 105: 295-304 (1994).
    • (1994) Plant Physiol , vol.105 , pp. 295-304
    • Hoffman, N.E.1    Franklin, A.E.2
  • 32
    • 0027532171 scopus 로고
    • Maturation of thylakoid lumen proteins proceeds post-translationally through an intermediate in vivo
    • Howe G, Merchant S: Maturation of thylakoid lumen proteins proceeds post-translationally through an intermediate in vivo. Proc Natl Acad Sci USA 90: 1862-1866 (1993).
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1862-1866
    • Howe, G.1    Merchant, S.2
  • 33
    • 0008365662 scopus 로고
    • Deletion mutants of chlorophyll a/b binding proteins are efficiently imported into chloroplasts but do not integrate into thylakoid membranes
    • Huang L, Adam Z, Hoffman NE: Deletion mutants of chlorophyll a/b binding proteins are efficiently imported into chloroplasts but do not integrate into thylakoid membranes. Plant Physiol 99: 247-255 (1992).
    • (1992) Plant Physiol , vol.99 , pp. 247-255
    • Huang, L.1    Adam, Z.2    Hoffman, N.E.3
  • 34
    • 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 RM, 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: 3251-3256 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 3251-3256
    • Hulford, A.1    Hazell, L.2    Mould, R.M.3    Robinson, C.4
  • 35
    • 0024341170 scopus 로고
    • Transport of proteins into chloroplasts: Import and maturation of precursors to the 33-, 23-, and 16-kDa proteins of the photosynthetic oxygen-evolving complex
    • James HE, Bartling D, Musgrove JE, Kirwin PM, Herrmann RG, Robinson C: Transport of proteins into chloroplasts: import and maturation of precursors to the 33-, 23-, and 16-kDa proteins of the photosynthetic oxygen-evolving complex. J Biol Chem 264: 19573-19576 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 19573-19576
    • James, H.E.1    Bartling, D.2    Musgrove, J.E.3    Kirwin, P.M.4    Herrmann, R.G.5    Robinson, C.6
  • 37
    • 0028556588 scopus 로고
    • The thylakoid translocation of subunit 3 of photosystem I, the psaF gene product, depends on a bipartite transit peptide and proceeds along an azide-sensitive pathway
    • Karnauchov I, Cai D, Schmidt I, Herrmann RG, Klösgen RB: The thylakoid translocation of subunit 3 of photosystem I, the psaF gene product, depends on a bipartite transit peptide and proceeds along an azide-sensitive pathway. J Biol Chem 269: 32871-32878 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 32871-32878
    • Karnauchov, I.1    Cai, D.2    Schmidt, I.3    Herrmann, R.G.4    Klösgen, R.B.5
  • 38
    • 0030953689 scopus 로고    scopus 로고
    • Negatively-charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane
    • Kiefer D, Xintong H, Dalbey R, Kuhn A: Negatively-charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane. EMBO J 16: 2197-2204 (1997).
    • (1997) EMBO J , vol.16 , pp. 2197-2204
    • Kiefer, D.1    Xintong, H.2    Dalbey, R.3    Kuhn, A.4
  • 39
    • 0030597984 scopus 로고    scopus 로고
    • An Arabidopsis thaliana cDNA encoding PSII-X, a 4.1 kDa component of photosystem II: A bipartite presequence mediates SecA/ΔpH-independent targeting into thylakoids
    • Kim SJ, Robinson D, Robinson C: An Arabidopsis thaliana cDNA encoding PSII-X, a 4.1 kDa component of photosystem II: a bipartite presequence mediates SecA/ΔpH-independent targeting into thylakoids. FEBS Lett 390: 175-178 (1996).
    • (1996) FEBS Lett , vol.390 , pp. 175-178
    • Kim, S.J.1    Robinson, D.2    Robinson, C.3
  • 40
    • 0032489422 scopus 로고    scopus 로고
    • Sec/SRP-independent insertion of two thylakoid membrane proteins bearing cleavable signal peptides
    • Kim SJ, Robinson C, Mant A: Sec/SRP-independent insertion of two thylakoid membrane proteins bearing cleavable signal peptides. FEBS Lett 424: 105-108 (1998).
    • (1998) FEBS Lett , vol.424 , pp. 105-108
    • Kim, S.J.1    Robinson, C.2    Mant, A.3
  • 41
    • 0024279608 scopus 로고
    • Transport of proteins into chloroplasts. Organization, orientation, and lateral distribution of the plastocyanin processing peptidase in the thylakoid network
    • Kirwin PM, Elderfield PD, Williams RS, Robinson C: Transport of proteins into chloroplasts. Organization, orientation, and lateral distribution of the plastocyanin processing peptidase in the thylakoid network. J Biol Chem 263: 18128-18132 (1988).
    • (1988) J Biol Chem , vol.263 , pp. 18128-18132
    • Kirwin, P.M.1    Elderfield, P.D.2    Williams, R.S.3    Robinson, C.4
  • 42
    • 0026828029 scopus 로고
    • Proton gradient-driven import of the 16kDa oxygen-evolving complex protein as the full precursor protein by isolated thylakoids
    • Klösgen RB, Brock IW, Herrmann RG, Robinson C: Proton gradient-driven import of the 16kDa oxygen-evolving complex protein as the full precursor protein by isolated thylakoids. Plant Mol Biol 18: 1031-1034 (1992).
    • (1992) Plant Mol Biol , vol.18 , pp. 1031-1034
    • Klösgen, R.B.1    Brock, I.W.2    Herrmann, R.G.3    Robinson, C.4
  • 43
    • 0028365045 scopus 로고
    • The SecA inhibitor, azide, reversibly blocks the translocation of a subset of lumenal proteins across the thylakoid membrane
    • Knott TG, Robinson C: The SecA inhibitor, azide, reversibly blocks the translocation of a subset of lumenal proteins across the thylakoid membrane. J Biol Chem 269: 7843-7846 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 7843-7846
    • Knott, T.G.1    Robinson, C.2
  • 44
    • 0024422740 scopus 로고
    • Targeting of proteins to the thylakoid lumen by the bipartite transit peptide of the 33kDa oxygen-evolving protein
    • Ko K, Cashmore AR: Targeting of proteins to the thylakoid lumen by the bipartite transit peptide of the 33kDa oxygen-evolving protein. EMBO J 8: 3187-3194 (1989).
    • (1989) EMBO J , vol.8 , pp. 3187-3194
    • Ko, K.1    Cashmore, A.R.2
  • 45
    • 77958418363 scopus 로고
    • Transport of proteins into the thylakoid lumen: Stromal processing and energy requirements for the import of the precursor to the 23 kDa protein of PSII
    • Konishi T, Watanabe A: Transport of proteins into the thylakoid lumen: stromal processing and energy requirements for the import of the precursor to the 23 kDa protein of PSII. Plant Cell Physiol 34: 315-319 (1993).
    • (1993) Plant Cell Physiol , vol.34 , pp. 315-319
    • Konishi, T.1    Watanabe, A.2
  • 46
    • 0029098779 scopus 로고
    • Major coat proteins of bacteriophage Pf3 and M13 as model systems for Sec-independent protein transport
    • Kuhn, A: Major coat proteins of bacteriophage Pf3 and M13 as model systems for Sec-independent protein transport. FEMS Micro Rev 17: 185-190 (1995).
    • (1995) FEMS Micro Rev , vol.17 , pp. 185-190
    • Kuhn, A.1
  • 47
    • 0023481543 scopus 로고
    • Nucleotide sequence of the gene from the cyanobacterium Anacystis nidulans R2 encoding the Mn-stabilising protein involved in photosystem II water oxidation
    • Kuwabara T, Reddy KJ, Sherman LA: Nucleotide sequence of the gene from the cyanobacterium Anacystis nidulans R2 encoding the Mn-stabilising protein involved in photosystem II water oxidation. Proc Natl Acad Sci USA 84: 8230-8234 (1987).
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8230-8234
    • Kuwabara, T.1    Reddy, K.J.2    Sherman, L.A.3
  • 48
    • 0029068677 scopus 로고
    • A SecY homolog in Arabidopsis thaliana. Sequence of a full-length cDNA clone and import of the precursor protein into chloroplasts
    • Laidler V, Chaddock AM, Knott TG, Walker D, Robinson C: A SecY homolog in Arabidopsis thaliana. Sequence of a full-length cDNA clone and import of the precursor protein into chloroplasts. J Biol Chem 270: 17664-17667 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 17664-17667
    • Laidler, V.1    Chaddock, A.M.2    Knott, T.G.3    Walker, D.4    Robinson, C.5
  • 49
    • 0024288942 scopus 로고
    • The chlorophyll a/b-binding protein inserts into the thylakoids independent of its cognate transit peptide
    • Lamppa, GK: The chlorophyll a/b-binding protein inserts into the thylakoids independent of its cognate transit peptide. J Biol Chem 263: 14996-14999 (1988).
    • (1988) J Biol Chem , vol.263 , pp. 14996-14999
    • Lamppa, G.K.1
  • 50
    • 0029041304 scopus 로고
    • A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the post-translational integration of a protein into thylakoid membranes
    • Li X, Henry R, Yuan J, Cline K, Hoffman NE: A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the post-translational integration of a protein into thylakoid membranes. Proc Natl Acad Sci USA 92: 3789-3793 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3789-3793
    • Li, X.1    Henry, R.2    Yuan, J.3    Cline, K.4    Hoffman, N.E.5
  • 52
    • 0028284220 scopus 로고
    • Mammalian and Escherichia coli signal recognition particles
    • Luirink JL, Dobberstein B: Mammalian and Escherichia coli signal recognition particles. Mol Microbiol 11: 9-13 (1994).
    • (1994) Mol Microbiol , vol.11 , pp. 9-13
    • Luirink, J.L.1    Dobberstein, B.2
  • 53
    • 0028239208 scopus 로고
    • The thylakoid-targeting domain of the chloroplast Rieske iron-sulphur protein is located in the N-terminal hydrophobic region of the mature protein
    • Madueño F, Bradshaw SA, Gray JC: The thylakoid-targeting domain of the chloroplast Rieske iron-sulphur protein is located in the N-terminal hydrophobic region of the mature protein. J Biol Chem 269: 17458-17463 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 17458-17463
    • Madueño, F.1    Bradshaw, S.A.2    Gray, J.C.3
  • 54
    • 0028063040 scopus 로고
    • Multiple mechanisms for the targeting of photosystem I subunits F, H, K, L, and N into and across the thylakoid membrane
    • Mant A, Nielsen VS, Knott TG, Møller BL, Robinson C: Multiple mechanisms for the targeting of photosystem I subunits F, H, K, L, and N into and across the thylakoid membrane. J Biol Chem 269: 27303-27309 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 27303-27309
    • Mant, A.1    Nielsen, V.S.2    Knott, T.G.3    Møller, B.L.4    Robinson, C.5
  • 55
    • 0028877047 scopus 로고
    • Sec-dependent thylakoid protein translocation. ΔpH requirement is dictated by passenger protein and ATP concentration
    • Mant A, Schmidt I, Herrmann RG, Robinson C, Klösgen RB: Sec-dependent thylakoid protein translocation. ΔpH requirement is dictated by passenger protein and ATP concentration. J Biol Chem 270: 23275-23281 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 23275-23281
    • Mant, A.1    Schmidt, I.2    Herrmann, R.G.3    Robinson, C.4    Klösgen, R.B.5
  • 56
    • 0032548799 scopus 로고    scopus 로고
    • An Arabidopsis cDNA encodes an apparent polyprotein of two non-identical thylakoid membrane proteins that are associated with photosystem II and homologous to algal ycf32 open reading frames
    • Mant A, Robinson C: An Arabidopsis cDNA encodes an apparent polyprotein of two non-identical thylakoid membrane proteins that are associated with photosystem II and homologous to algal ycf32 open reading frames. FEBS Lett 423: 183-188 (1998).
    • (1998) FEBS Lett , vol.423 , pp. 183-188
    • Mant, A.1    Robinson, C.2
  • 57
    • 0028261428 scopus 로고
    • Targeting of proteins to thylakoids by bipartite presequences: CFoII is imported by a novel, third pathway
    • Michl D, Robinson C, Shackleton JB, Herrmann RG, Klösgen RB: Targeting of proteins to thylakoids by bipartite presequences: CFoII is imported by a novel, third pathway. EMBO J 13: 1310-1317 (1994).
    • (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
  • 58
    • 0025781325 scopus 로고
    • A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane
    • Mould RM, Robinson C: 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).
    • (1991) J Biol Chem , vol.266 , pp. 12189-12193
    • Mould, R.M.1    Robinson, C.2
  • 59
    • 0031149916 scopus 로고    scopus 로고
    • Azide-sensitive thylakoid membrane insertion of chimeric cytochrome f constructs imported by isolated pea chloroplasts
    • Mould RM, Knight JS, Bogsch E, Gray JC: Azide-sensitive thylakoid membrane insertion of chimeric cytochrome f constructs imported by isolated pea chloroplasts. Plant J 11: 1051-1058 (1997).
    • (1997) Plant J , vol.11 , pp. 1051-1058
    • Mould, R.M.1    Knight, J.S.2    Bogsch, E.3    Gray, J.C.4
  • 60
    • 0027336391 scopus 로고
    • SecY protein is localised in both the cytoplasmic and thylakoid membranes in the cyanobacterium Synechococcus PCC7942
    • Nakai M, Sugita D, Omata T, Endo T: SecY protein is localised in both the cytoplasmic and thylakoid membranes in the cyanobacterium Synechococcus PCC7942. Biochem Biophys Res Comm 193: 228-234 (1993).
    • (1993) Biochem Biophys Res Comm , vol.193 , pp. 228-234
    • Nakai, M.1    Sugita, D.2    Omata, T.3    Endo, T.4
  • 61
    • 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, Endo T: Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J Biol Chem 269: 31338-31341 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 31338-31341
    • Nakai, M.1    Goto, A.2    Nohara, T.3    Sugita, D.4    Endo, T.5
  • 62
    • 0028169710 scopus 로고
    • Import of barley photosystem I subunit N into the thylakoid lumen is mediated by a bipartite presequence lacking an intermediate cleavage site: Role of the delta pH in translocation across the thylakoid membrane
    • Nielsen VS, Mant A, Knoetzel J, Møller BL, Robinson C: Import of barley photosystem I subunit N into the thylakoid lumen is mediated by a bipartite presequence lacking an intermediate cleavage site: role of the delta pH in translocation across the thylakoid membrane. J Biol Chem 269: 3762-3766 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 3762-3766
    • Nielsen, V.S.1    Mant, A.2    Knoetzel, J.3    Møller, B.L.4    Robinson, C.5
  • 63
    • 0030590083 scopus 로고    scopus 로고
    • Cytochrome f encoded by the chloroplast genome is imported into thylakoids via the SecA-dependent pathway
    • Nohara T, Asai T, Nakai M, Sugiura M, Endo T: Cytochrome f encoded by the chloroplast genome is imported into thylakoids via the SecA-dependent pathway. Biochem Biophys Res Comm 224: 474-478 (1996).
    • (1996) Biochem Biophys Res Comm , vol.224 , pp. 474-478
    • Nohara, T.1    Asai, T.2    Nakai, M.3    Sugiura, M.4    Endo, T.5
  • 64
    • 0025087137 scopus 로고
    • Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
    • Oliver DB, Cabelli RJ, Dolan KM, Jarosuk GP: Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc Natl Acad Sci USA 87: 8227-8231 (1990).
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8227-8231
    • Oliver, D.B.1    Cabelli, R.J.2    Dolan, K.M.3    Jarosuk, G.P.4
  • 65
    • 0026071203 scopus 로고
    • A stromal protein factor maintains the solubility and insertion competence of an imported thylakoid membrane protein
    • Payan LA, Cline K: A stromal protein factor maintains the solubility and insertion competence of an imported thylakoid membrane protein. J Cell Biol 112: 603-613 (1991).
    • (1991) J Cell Biol , vol.112 , pp. 603-613
    • Payan, L.A.1    Cline, K.2
  • 66
    • 0027980013 scopus 로고
    • The presequence of a chimeric construct dictates which of two mechanisms is utilised for translocation across the thylakoid membrane: Evidence for the existence of two distinct translocation systems
    • Robinson C, Cai D, Hulford A, Brock IW, Michl D, Hazell L, Schmidt I, Herrmann RG, Klösgen RB: The presequence of a chimeric construct dictates which of two mechanisms is utilised for translocation across the thylakoid membrane: evidence for the existence of two distinct translocation systems. EMBO J 13: 279-285 (1994).
    • (1994) EMBO J , vol.13 , pp. 279-285
    • Robinson, C.1    Cai, D.2    Hulford, A.3    Brock, I.W.4    Michl, D.5    Hazell, L.6    Schmidt, I.7    Herrmann, R.G.8    Klösgen, R.B.9
  • 68
    • 0029846723 scopus 로고    scopus 로고
    • Analysis of the import of carboxy-terminal truncations of the 23-kilodalton subunit of the oxygen-evolving complex suggests that its structure is an important determinant for thylakoid transport
    • Roffey RA, Theg SM: Analysis of the import of carboxy-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: 1329-1338 (1996).
    • (1996) Plant Physiol , vol.111 , pp. 1329-1338
    • Roffey, R.A.1    Theg, S.M.2
  • 69
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini C-L, Ize B, Chanal A, Müller M, Giordano G, Wu L-F: A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J 17: 101-112 (1998).
    • (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
  • 70
    • 0026713541 scopus 로고
    • Identification of a chloroplast-encoded secA gene homologue in a chromophytic alga: Possible role in chloroplast protein translocation
    • Scaramuzzi CD, Hiller RG, Stokes HW: Identification of a chloroplast-encoded secA gene homologue in a chromophytic alga: possible role in chloroplast protein translocation. Curr Genet 22: 421-426 (1992).
    • (1992) Curr Genet , vol.22 , pp. 421-426
    • Scaramuzzi, C.D.1    Hiller, R.G.2    Stokes, H.W.3
  • 71
    • 0025297347 scopus 로고
    • Expression in Escherichia coli of the psbO gene encoding the 33 kd protein of the oxygen-evolving complex from spinach
    • Seidler A, Michel H: Expression in Escherichia coli of the psbO gene encoding the 33 kd protein of the oxygen-evolving complex from spinach. EMBO J 9: 1743-1748 (1990).
    • (1990) EMBO J , vol.9 , pp. 1743-1748
    • Seidler, A.1    Michel, H.2
  • 73
    • 0022763140 scopus 로고
    • The role of the transit peptide in the routing of precursors toward different chloroplast compartments
    • Smeekens S, Bauerle C, Hageman J, Keegstra K, Weisbeek P: The role of the transit peptide in the routing of precursors toward different chloroplast compartments. Cell 46: 365-375 (1986).
    • (1986) Cell , vol.46 , pp. 365-375
    • Smeekens, S.1    Bauerle, C.2    Hageman, J.3    Keegstra, K.4    Weisbeek, P.5
  • 75
    • 0031472242 scopus 로고    scopus 로고
    • The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt ND, Newitt JA, Bernstein HD: The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88: 187-196 (1997).
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 76
    • 0027530587 scopus 로고
    • SecA is plastid-encoded in a red alga: Implications for the evolution of plastid genomes and the thylakoid protein import apparatus
    • Valentin, K: SecA is plastid-encoded in a red alga: implications for the evolution of plastid genomes and the thylakoid protein import apparatus. Mol Gen Genet 236: 245 (1993).
    • (1993) Mol Gen Genet , vol.236 , pp. 245
    • Valentin, K.1
  • 77
    • 0345611654 scopus 로고
    • A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases
    • van der Vere PS, Bennett TM, Oblong JE, Lamppa GK: A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases. Proc Natl Acad Sci USA 92: 7177-7181 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7177-7181
    • Van Der Vere, P.S.1    Bennett, T.M.2    Oblong, J.E.3    Lamppa, G.K.4
  • 78
    • 0024288943 scopus 로고
    • What is the role of the transit peptide in thylakoid integration of the light-harvesting chlorophyll a/b protein?
    • Viitanen PV, Doran ER, Dunsmuir P: What is the role of the transit peptide in thylakoid integration of the light-harvesting chlorophyll a/b protein? J Biol Chem 263: 15000-15007 (1988).
    • (1988) J Biol Chem , vol.263 , pp. 15000-15007
    • Viitanen, P.V.1    Doran, E.R.2    Dunsmuir, P.3
  • 79
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker R, Barkan A: Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J 14: 3905-3914 (1995).
    • (1995) EMBO J , vol.14 , pp. 3905-3914
    • Voelker, R.1    Barkan, A.2
  • 80
    • 0031014540 scopus 로고    scopus 로고
    • Transposon-Disruption of a maize nuclear gene, tha1, encoding a chloroplast SecA homologue: In vivo role of cp-SecA in thylakoid protein targeting
    • Voelker R, Mendel-Hartvig J, Barkan A: Transposon-Disruption of a maize nuclear gene, tha1, encoding a chloroplast SecA homologue: in vivo role of cp-SecA in thylakoid protein targeting. Genetics 145: 467-478 (1997).
    • (1997) Genetics , vol.145 , pp. 467-478
    • Voelker, R.1    Mendel-Hartvig, J.2    Barkan, A.3
  • 81
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Herrmann RG: Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535-545 (1989).
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 82
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne G: Membrane proteins: from sequence to structure. Annu Rev Biophys Biomol Struct 23: 167-192 (1994).
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 84
    • 0027961026 scopus 로고
    • SecA homolog in protein transport within chloroplasts: Evidence for endosymbiont-derived sorting
    • Yuan J, Henry R, McCaffery M, Cline K: SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting. Science 266: 796-798 (1994).
    • (1994) Science , vol.266 , pp. 796-798
    • Yuan, J.1    Henry, R.2    McCaffery, M.3    Cline, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.