메뉴 건너뛰기




Volumn 49, Issue , 1998, Pages 97-126

Protein targeting to the thylakoid membrane

Author keywords

Choroplast; Organelle biogenesis; Protein translocation; Signal peptide; Transit sequence

Indexed keywords


EID: 0031788952     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.49.1.97     Document Type: Article
Times cited : (58)

References (157)
  • 1
    • 0000686288 scopus 로고
    • Properties of a chloroplast enzyme that cleaves the chlorophyll a/b binding protein precursor
    • AbadMS,ClarkSE,LamppaGK. 1989. Properties of a chloroplast enzyme that cleaves the chlorophyll a/b binding protein precursor. Plant Physiol. 90:117-24
    • (1989) Plant Physiol. , vol.90 , pp. 117-124
    • Abad, M.S.1    Clark, S.E.2    Lamppa, G.K.3
  • 2
    • 0028028792 scopus 로고
    • Methotrexate does not block import of a DHFR fusion protein into chlomplasts
    • 1a. America T, Hageman J, Guéra A, Rook F, Archer K, et al. 1994. Methotrexate does not block import of a DHFR fusion protein into chlomplasts. Plant Mol. Biol. 24:283-94
    • (1994) Plant Mol. Biol. , vol.24 , pp. 283-294
    • America, T.1    Hageman, J.2    Guéra, A.3    Rook, F.4    Archer, K.5
  • 3
    • 0025975025 scopus 로고
    • Cleavage of the precursor of pea chloroplast cytocnrome f by leader peptidase from Escherichia coli
    • Anderson CM, Gray J. 1991. Cleavage of the precursor of pea chloroplast cytocnrome f by leader peptidase from Escherichia coli. FEBS Lett. 280:383-86
    • (1991) FEBS Lett. , vol.280 , pp. 383-386
    • Anderson, C.M.1    Gray, J.2
  • 4
    • 0029963973 scopus 로고    scopus 로고
    • Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
    • Bacher G, Lütcke H, Jungnickel B, Rapaport TA, Dobberstein B. 1996. Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Nature 381:248-51
    • (1996) Nature , vol.381 , pp. 248-251
    • Bacher, G.1    Lütcke, H.2    Jungnickel, B.3    Rapaport, T.A.4    Dobberstein, B.5
  • 5
    • 0029780761 scopus 로고    scopus 로고
    • Hydrophobie core but not amino-terminal charged residues are required for translocation of an integral thylakoid membrane protein in vivo
    • Baillet B, Kohorn BD. 1996. Hydrophobie core but not amino-terminal charged residues are required for translocation of an integral thylakoid membrane protein in vivo. J. Biol. Chem. 271:18375-78
    • (1996) J. Biol. Chem. , vol.271 , pp. 18375-18378
    • Baillet, B.1    Kohorn, B.D.2
  • 6
    • 0022742587 scopus 로고
    • Chloroplast gene expression in nuclear photosynthetic mutants of maize
    • Barkan A, Miles D, Taylor W. 1986. Chloroplast gene expression in nuclear photosynthetic mutants of maize. EMBO J. 5:1421-27
    • (1986) EMBO J. , vol.5 , pp. 1421-1427
    • Barkan, A.1    Miles, D.2    Taylor, W.3
  • 8
    • 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, Battling D, Mould RM, Dunbar B, Weisbeek P, et al. 1991. 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. 266:23606-10
    • (1991) J. Biol. Chem. , vol.266 , pp. 23606-23610
    • Bassham, D.C.1    Battling, D.2    Mould, R.M.3    Dunbar, B.4    Weisbeek, P.5
  • 9
    • 0026000240 scopus 로고
    • Kinetic analysis of the transport of thylakoid lumenal proteins in experiments using intact chloroplasts
    • Bauerle C, Dorl J, Keegstra K. 1991. Kinetic analysis of the transport of thylakoid lumenal proteins in experiments using intact chloroplasts. J. Biol Chem. 266:5884-90
    • (1991) J. Biol Chem. , vol.266 , pp. 5884-5890
    • Bauerle, C.1    Dorl, J.2    Keegstra, K.3
  • 10
    • 0026077470 scopus 로고
    • Full-length plastocyanin precursor is translocated across isolated thylakoid membranes
    • Bauerle C, Keegstra K. 1991. Full-length plastocyanin precursor is translocated across isolated thylakoid membranes. J. Biol. Chem. 266:5876-83
    • (1991) J. Biol. Chem. , vol.266 , pp. 5876-5883
    • Bauerle, C.1    Keegstra, K.2
  • 11
    • 0029129564 scopus 로고
    • Isolation and characterization of a cDNA encoding the SecA protein from spinach chloroplasts
    • Berghöfer J, Karnauchov I, Herrmann RG, Klösgen RB. 1995. Isolation and characterization of a cDNA encoding the SecA protein from spinach chloroplasts. J. Biol. Chem. 270:18341-46
    • (1995) J. Biol. Chem. , vol.270 , pp. 18341-18346
    • Berghöfer, J.1    Karnauchov, I.2    Herrmann, R.G.3    Klösgen, R.B.4
  • 12
    • 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, Robinson C. 1997. 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. 16:3851-59
    • (1997) EMBO J. , vol.16 , pp. 3851-3859
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 13
    • 0030978698 scopus 로고    scopus 로고
    • Unusual characteristics of amino-terminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides
    • Brink S, Bogsch EG, Mant A, Robinson C. 1997. Unusual characteristics of amino-terminal and hydrophobic domains in nuclear-encoded thylakoid signal peptides. Ear. J. Biochem. 245:340-48
    • (1997) Ear. J. Biochem. , vol.245 , pp. 340-348
    • Brink, S.1    Bogsch, E.G.2    Mant, A.3    Robinson, C.4
  • 14
    • 0027690206 scopus 로고
    • Precursors of one integral and five lumenal thylakoid proteins are imported by isolated pea and barley thylakoids: Optimisation of in vitro assays
    • Brock IW, Hazell L, Michl D, Nielsen WS, Møller BL, et al. 1993. Precursors of one integral and five lumenal thylakoid proteins are imported by isolated pea and barley thylakoids: optimisation of in vitro assays. Plant Mol. Biol. 23:717-25
    • (1993) Plant Mol. Biol. , vol.23 , pp. 717-725
    • Brock, I.W.1    Hazell, L.2    Michl, D.3    Nielsen, W.S.4    Møller, B.L.5
  • 15
    • 0028985671 scopus 로고
    • The delta pH-driven, ATP-independent protein translocation mechanism in the chloroplast thylakoid membrane: Kinetics and energetics
    • Brock IW, Mills JD, Robinson D, Robinson C. 1995. The delta pH-driven, ATP-independent protein translocation mechanism in the chloroplast thylakoid membrane: kinetics and energetics. J . Biol. Chem. 270:1657-62
    • (1995) J . Biol. Chem. , vol.270 , pp. 1657-1662
    • Brock, I.W.1    Mills, J.D.2    Robinson, D.3    Robinson, C.4
  • 16
    • 0024969262 scopus 로고
    • A truncated analog of a prelight-harvesting chlorophyll a/b protein II transit peptide inhibits protein import into chloroplasts
    • Buvinger WE, Michel H, Bennett J. 1989. A truncated analog of a prelight-harvesting chlorophyll a/b protein II transit peptide inhibits protein import into chloroplasts. J. Biol. Chem. 264: 1195-202
    • (1989) J. Biol. Chem. , vol.264 , pp. 1195-1202
    • Buvinger, W.E.1    Michel, H.2    Bennett, J.3
  • 17
    • 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. 1993. 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. 3:383-92
    • (1993) Plant J. , vol.3 , pp. 383-392
    • Cai, D.1    Herrmann, R.G.2    Klösgen, R.B.3
  • 18
    • 0001682178 scopus 로고
    • Structure and expression of a pea nuclear gene encoding a chlorophyll a/b-binding polypeptide
    • Cashmore AR. 1984. Structure and expression of a pea nuclear gene encoding a chlorophyll a/b-binding polypeptide. Proc. Natl. Acad. Sci. USA 81:2960-64
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2960-2964
    • Cashmore, A.R.1
  • 19
    • 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 AM, Mant A, Karnauchov I, Brink S, Herrmann RG, et al. 1995. 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. 14:2715-22
    • (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
  • 20
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • Chirico WJ, Waters MG, Blobel G. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 322:805-10
    • (1988) Nature , vol.322 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 21
    • 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. 1987. 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) Plant Mol. Biol. , vol.10 , pp. 3-11
    • Chitnis, P.R.1    Nechushtai, R.2    Thornber, J.P.3
  • 22
    • 0024971457 scopus 로고
    • Mutations at the transit peptide-mature protein junction separate two cleavage events during chloroplast import of the chlorophyll a/b-binding protein
    • Clark SE, Abad MS, Lamppa GK. 1989. Mutations at the transit peptide-mature protein junction separate two cleavage events during chloroplast import of the chlorophyll a/b-binding protein. J. Biol. Chem. 264:17544-50
    • (1989) J. Biol. Chem. , vol.264 , pp. 17544-17550
    • Clark, S.E.1    Abad, M.S.2    Lamppa, G.K.3
  • 23
    • 0025376571 scopus 로고
    • Loss of efficient import and thylakoid insertion due to N- And C-terminal deletions in the light-harvesting chlorophyll a/b binding protein
    • Clark SE, Oblong JE, Lamppa GK. 1990. Loss of efficient import and thylakoid insertion due to N- and C-terminal deletions in the light-harvesting chlorophyll a/b binding protein. Plant Cell 2:173-84
    • (1990) Plant Cell , vol.2 , pp. 173-184
    • Clark, S.E.1    Oblong, J.E.2    Lamppa, G.K.3
  • 24
    • 0030918441 scopus 로고    scopus 로고
    • A folded protein can be transported across the chloroplast envelope and thylakoid membranes
    • 21a. Clark SA, Theg SM. 1997. A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol. Biol. Cell 8:923-34
    • (1997) Mol. Biol. Cell , vol.8 , pp. 923-934
    • Clark, S.A.1    Theg, S.M.2
  • 25
    • 0027238554 scopus 로고
    • Protein import into chloro- Plasts: The hydrophilic lumenal proteins exhibit unexpected import and sorting specificities in spite of structurally conserved transit peptides
    • Clausmeyer S, Klösgen RB, Herrmann RG. 1993. Protein import into chloro- plasts: the hydrophilic lumenal proteins exhibit unexpected import and sorting specificities in spite of structurally conserved transit peptides. J. Biol. Chem. 268:13869-76
    • (1993) J. Biol. Chem. , vol.268 , pp. 13869-13876
    • Clausmeyer, S.1    Klösgen, R.B.2    Herrmann, R.G.3
  • 26
    • 0022851237 scopus 로고
    • Import of proteins into chloroplasts: Membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates
    • Cline K. 1986. Import of proteins into chloroplasts: membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates. J. Biol. Chem. 261:14804-10
    • (1986) J. Biol. Chem. , vol.261 , pp. 14804-14810
    • Cline, K.1
  • 27
    • 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. 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. 267:2688-96
    • (1992) J. Biol. Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 28
    • 0024978446 scopus 로고
    • An imported thylakoid protein accumulates in the stroma when insertion into thylakoids is inhibited
    • Cline K, Fulsom DR, Viitanen PV. 1989. An imported thylakoid protein accumulates in the stroma when insertion into thylakoids is inhibited. J. Biol. Chem. 264:14225-32
    • (1989) J. Biol. Chem. , vol.264 , pp. 14225-14232
    • Cline, K.1    Fulsom, D.R.2    Viitanen, P.V.3
  • 29
    • 0029731659 scopus 로고    scopus 로고
    • Import and routing of nucleus-encoded chloroplast proteins
    • Cline K, Henry R. 1996. Import and routing of nucleus-encoded chloroplast proteins. Anna. Rev. Cell Dev. Biol. 12:1-26
    • (1996) Anna. Rev. Cell Dev. Biol. , vol.12 , pp. 1-26
    • Cline, K.1    Henry, R.2
  • 30
    • 0347937778 scopus 로고
    • Pathways and intermediates for the biogenesis of nuclear-encoded thylakoid proteins
    • ed. N Murata. Dordrecht: Kluwer
    • Cline K, Henry R, Li CJ, Yuan JG. 1992. Pathways and intermediates for the biogenesis of nuclear-encoded thylakoid proteins. In Research in Photosynthesis, ed. N Murata, pp. 149-56. Dordrecht: Kluwer
    • (1992) Research in Photosynthesis , pp. 149-156
    • Cline, K.1    Henry, R.2    Li, C.J.3    Yuan, J.G.4
  • 31
    • 0027494820 scopus 로고
    • Multiple pathways for protein transport into or across the thylakoid membrane
    • Cline K, Henry R, Li CJ, Yuan JG. 1993. Multiple pathways for protein transport into or across the thylakoid membrane. EMBOJ. 12:4105-14
    • (1993) EMBOJ , vol.12 , pp. 4105-4114
    • Cline, K.1    Henry, R.2    Li, C.J.3    Yuan, J.G.4
  • 32
    • 0022431959 scopus 로고
    • Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts
    • Cline K, Werner-Washburne M, Lubben TH, Keegstra K. 1985. Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts. J. Biol. Chem. 260:3691-96
    • (1985) J. Biol. Chem. , vol.260 , pp. 3691-3696
    • Cline, K.1    Werner-Washburne, M.2    Lubben, T.H.3    Keegstra, K.4
  • 33
    • 0029017359 scopus 로고
    • Integration and assembly of photosynthetic protein complexes in chloroplast thylakoid membranes
    • Cohen Y, Yalovsky S, Nechushtai R. 1995. Integration and assembly of photosynthetic protein complexes in chloroplast thylakoid membranes. Biochim. Biophys. Acta 1241:1-30
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 1-30
    • Cohen, Y.1    Yalovsky, S.2    Nechushtai, R.3
  • 34
    • 0028945041 scopus 로고
    • A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoid protein transport pathway
    • Creighton AM, Hulford A, Mant A, Robinson D, Robinson C. 1995. A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoid protein transport pathway. J. Biol. Chem. 270:1663-69
    • (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
  • 35
    • 0026047161 scopus 로고
    • Chloroplast protein topogenesis: Import, sorting and assembly
    • De Boer AD, Weisbeek PJ. 1991. Chloroplast protein topogenesis: import, sorting and assembly. Biochim. Biophys. Acta 1071:221-53
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 221-253
    • De Boer, A.D.1    Weisbeek, P.J.2
  • 36
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies R, Koch B, Werner-Washburne M, Craig E, Schekman R. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332:800-5
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.1    Koch, B.2    Werner-Washburne, M.3    Craig, E.4    Schekman, R.5
  • 37
    • 0028338910 scopus 로고
    • Characterization of the gene of the chloroplast Rieske iron-sulfur protein in Chlamydomonas reinhardtii
    • De Vitry C. 1994. Characterization of the gene of the chloroplast Rieske iron-sulfur protein in Chlamydomonas reinhardtii. J. Biol. Chem. 269:7603-9
    • (1994) J. Biol. Chem. , vol.269 , pp. 7603-7609
    • De Vitry, C.1
  • 38
    • 0028017537 scopus 로고
    • Chloroplast protein import: Chloroplast envelopes and thylakoids have different abilities to unfold proteins
    • 34a. Endo T, Kawakami M, Gogo A, America T, Weisbeek P, Nakai M. 1994. Chloroplast protein import: chloroplast envelopes and thylakoids have different abilities to unfold proteins. Eur. J. Biochem. 225:403-9
    • (1994) Eur. J. Biochem. , vol.225 , pp. 403-409
    • Endo, T.1    Kawakami, M.2    Gogo, A.3    America, T.4    Weisbeek, P.5    Nakai, M.6
  • 39
    • 0027476967 scopus 로고
    • Sec Y, an integral subunit of the bacterial preprotein translocase, is encoded by a plastid genome
    • Flachmann R, Michalowski CB, Löffelhardt W, Bohnert HJ. 1993. Sec Y, an integral subunit of the bacterial preprotein translocase, is encoded by a plastid genome. J. Biol Chem. 268:7514-19
    • (1993) J. Biol Chem. , vol.268 , pp. 7514-7519
    • Flachmann, R.1    Michalowski, C.B.2    Löffelhardt, W.3    Bohnert, H.J.4
  • 40
    • 0027377619 scopus 로고
    • Characterization of a chloroplast homologue of the 54-kDa subunit of the signal recognition particle
    • Franklin AE, Hoffman NE. 1993. Characterization of a chloroplast homologue of the 54-kDa subunit of the signal recognition particle. J. Biol. Chem. 268:22175-80
    • (1993) J. Biol. Chem. , vol.268 , pp. 22175-22180
    • Franklin, A.E.1    Hoffman, N.E.2
  • 41
    • 0000262786 scopus 로고
    • Chloroplast protein import: Quantitative analysis of precursor binding
    • Friedman AL, Keegstra K. 1989. Chloroplast protein import: quantitative analysis of precursor binding. Plant Physiol. 89:993-99
    • (1989) Plant Physiol. , vol.89 , pp. 993-999
    • Friedman, A.L.1    Keegstra, K.2
  • 42
    • 0031397350 scopus 로고    scopus 로고
    • Mechanism of protein-transport across the chloroplast envelope
    • Fuks B, Schnell DJ. 1997. Mechanism of protein-transport across the chloroplast envelope. Plant Physiol. 114:405-10
    • (1997) Plant Physiol. , vol.114 , pp. 405-410
    • Fuks, B.1    Schnell, D.J.2
  • 43
    • 0009575273 scopus 로고
    • A soluble protein factor is required in vitro for membrane insertion of the thylakoid precursor protein, pLHCR
    • Fulson DR, Cline K. 1988. A soluble protein factor is required in vitro for membrane insertion of the thylakoid precursor protein, pLHCR Plant Physiol. 88:1146-53
    • (1988) Plant Physiol. , vol.88 , pp. 1146-1153
    • Fulson, D.R.1    Cline, K.2
  • 44
    • 0029038943 scopus 로고
    • Protein translocation across chloroplast envelope membranes
    • Gray J, Row PE. 1995. Protein translocation across chloroplast envelope membranes. Trends Cell Biol. 5:243-7
    • (1995) Trends Cell Biol. , vol.5 , pp. 243-247
    • Gray, J.1    Row, P.E.2
  • 45
    • 0027674916 scopus 로고
    • A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes
    • 40a. Guéra A, America T, van Waas M, Weisbeek PJ. 1993. A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes. Plant Mol. Biol 23:309-34
    • (1993) Plant Mol. Biol , vol.23 , pp. 309-334
    • Guéra, A.1    America, T.2    Van Waas, M.3    Weisbeek, P.J.4
  • 48
    • 0001610085 scopus 로고
    • A thylakoid-located processing protease is required for complete maturation of the lumen protein plastocyanin
    • Hageman J, Robinson C, Smeekens S, Weisbeek P. 1986. A thylakoid-located processing protease is required for complete maturation of the lumen protein plastocyanin. Nature 324:567-69
    • (1986) Nature , vol.324 , pp. 567-569
    • Hageman, J.1    Robinson, C.2    Smeekens, S.3    Weisbeek, P.4
  • 49
    • 0024852098 scopus 로고
    • The reaction specificities of the thylakoid processing peptidase and Escherichia coli leader peptidase are iden- Tical
    • Halpin C, Elderfield PD, James HE, Zimmermann R, Dunbar B, Robinson C. 1989. The reaction specificities of the thylakoid processing peptidase and Escherichia coli leader peptidase are iden- tical. EMBO J. 8:3917-21
    • (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
  • 50
    • 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. 1989. The transit peptide of a chloroplast thylakoid membrane protein is functionally equivalent to a stromal-targeting sequence. EMBO J. 8:3195-206
    • (1989) EMBO J. , vol.8 , pp. 3195-3206
    • Hand, J.M.1    Szabo, L.J.2    Vasconcelos, A.C.3    Cashmore, A.R.4
  • 51
    • 0031035488 scopus 로고    scopus 로고
    • Targeting determinants and proposed evolutionary basis for the Sec and delta-pH protein transport systems in chloroplast thylakoid membranes
    • Henry R, Carrigan M, McCaffery M, Ma XY, Cline K. 1997. Targeting determinants and proposed evolutionary basis for the Sec and delta-pH protein transport systems in chloroplast thylakoid membranes. J Cell Biol. 136:823-32
    • (1997) J Cell Biol. , vol.136 , pp. 823-832
    • Henry, R.1    Carrigan, M.2    McCaffery, M.3    Ma, X.Y.4    Cline, K.5
  • 52
    • 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. 1994. Differences between lumen targeting domains of chloroplast transit peptides determine pathway specificity for thylakoid transport. J. Biol. Chem. 269:10189-92
    • (1994) J. Biol. Chem. , vol.269 , pp. 10189-10192
    • Henry, R.1    Kapazoglou, A.2    McCaffery, M.3    Cline, K.4
  • 54
    • 0030937725 scopus 로고    scopus 로고
    • Chloroplast SRP54 interacts with a specific subset of thylakoid precursor proteins
    • High S, Henry R, Mould RM, Valent Q, Meacock S, et al. 1997. Chloroplast SRP54 interacts with a specific subset of thylakoid precursor proteins. J. Biol. Chem. 272:11622-28
    • (1997) J. Biol. Chem. , vol.272 , pp. 11622-11628
    • High, S.1    Henry, R.2    Mould, R.M.3    Valent, Q.4    Meacock, S.5
  • 55
    • 0028584270 scopus 로고
    • A receptor component of the chloroplast protein translocation machinery
    • Hirsch S, Muckel E, Heemeyer F, von Heijne G, Soll J. 1994. A receptor component of the chloroplast protein translocation machinery. Science 266:1989-92
    • (1994) Science , vol.266 , pp. 1989-1992
    • Hirsch, S.1    Muckel, E.2    Heemeyer, F.3    Von Heijne, G.4    Soll, J.5
  • 56
    • 0028430193 scopus 로고
    • Evidence for a stromal GTP requirement for the integration of a chlorophyll a/b-binding polypeptide into thylakoid membranes
    • Huffman NE, Franklin AE. 1994. 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) Plant Physiol , vol.105 , pp. 295-304
    • Huffman, N.E.1    Franklin, A.E.2
  • 57
    • 0027532171 scopus 로고
    • Maturation of thylakoid lumen proteins proceeds post-translationally through an intermediate in vivo
    • Howe G, Merchant S. 1993. Maturation of thylakoid lumen proteins proceeds post-translationally through an intermediate in vivo. Proc. Natl. Acad. Sci. USA 90:1862-66
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1862-1866
    • Howe, G.1    Merchant, S.2
  • 58
    • 0008365662 scopus 로고
    • Deletion mutants of chlorophyll a/b binding proteins are efficiently imported into chloroplasts but do not integrate into thylakoid membranes
    • Huang LQ, Adam Z, Hoffman NE. 1992. Deletion mutants of chlorophyll a/b binding proteins are efficiently imported into chloroplasts but do not integrate into thylakoid membranes. Plant Physiol. 99:247-55
    • (1992) Plant Physiol. , vol.99 , pp. 247-255
    • Huang, L.Q.1    Adam, Z.2    Hoffman, N.E.3
  • 59
    • 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. 1994. 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. 269:3251-56
    • (1994) J. Biol. Chem. , vol.269 , pp. 3251-3256
    • Hulford, A.1    Hazell, L.2    Mould, R.M.3    Robinson, C.4
  • 60
    • 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, Battling D, Musgrove JE, Kirwin PM, Herrmann RG, Robinson C. 1989. 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: 19573-76
    • (1989) J. Biol Chem , vol.264 , pp. 19573-19576
    • James, H.E.1    Battling, D.2    Musgrove, J.E.3    Kirwin, P.M.4    Herrmann, R.G.5    Robinson, C.6
  • 61
    • 0001067141 scopus 로고
    • Nucleotide sequence of cDNA clones encoding complete "23 kDa" and "16 kDa" precursor proteins associated with the photosynthetic oxygen-evolving complex from spinach
    • Jansen T, Rother C, Steppuhn J, Reinke H, Bayreuther K, et al. 1987. Nucleotide sequence of cDNA clones encoding complete "23 kDa" and "16 kDa" precursor proteins associated with the photosynthetic oxygen-evolving complex from spinach. FEBS Lett. 216:234-40
    • (1987) FEBS Lett. , vol.216 , pp. 234-240
    • Jansen, T.1    Rother, C.2    Steppuhn, J.3    Reinke, H.4    Bayreuther, K.5
  • 62
    • 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. 1994. 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. 269:32871-78
    • (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
  • 63
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries in the chloroplast
    • Kessler F, Blobel G. 1996. Interaction of the protein import and folding machineries in the chloroplast. Proc. Natl. Acad. Sci. USA 93:7684-89
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 64
    • 0027984260 scopus 로고
    • Identification of two GTP-binding proteins in the chloroplast protein import machinery
    • Kessler F, Blobel G, Patel HA, Schnell DJ. 1994. Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science 266: 1035-39
    • (1994) Science , vol.266 , pp. 1035-1039
    • Kessler, F.1    Blobel, G.2    Patel, H.A.3    Schnell, D.J.4
  • 65
    • 0030597984 scopus 로고    scopus 로고
    • An Arabidopsis thaliana cDNA encoding PS II-X, a 4.1 kDa component of photosystem II: A bipartite presequence mediates SecA/delta pH-independent targeting into thylakoids
    • Kim SJ, Robinson D, Robinson C. 1996. An Arabidopsis thaliana cDNA encoding PS II-X, a 4.1 kDa component of photosystem II: a bipartite presequence mediates SecA/delta pH-independent targeting into thylakoids. FEBS Lett. 390:175-78
    • (1996) FEBS Lett. , vol.390 , pp. 175-178
    • Kim, S.J.1    Robinson, D.2    Robinson, C.3
  • 67
    • 0023881275 scopus 로고
    • Light-regulated translation of chloroplast proteins. I. Transcripts of PsaA-PsaB, psbA, and RbcL are associated with polysemes in dark-grown and illuminated barley seedlings
    • Klein RR, Mason HS, Mullet JE. 1988. Light-regulated translation of chloroplast proteins. I. Transcripts of PsaA-PsaB, psbA, and RbcL are associated with polysemes in dark-grown and illuminated barley seedlings. J. Cell Biol. 106:289-301
    • (1988) J. Cell Biol. , vol.106 , pp. 289-301
    • Klein, R.R.1    Mason, H.S.2    Mullet, J.E.3
  • 68
    • 0242612480 scopus 로고    scopus 로고
    • Protein transport into and across the thylakoid membrane
    • Klösgen RB. 1997. Protein transport into and across the thylakoid membrane. J. Photochem. Photobiol. 38:1-9
    • (1997) J. Photochem. Photobiol. , vol.38 , pp. 1-9
    • Klösgen, R.B.1
  • 69
    • 0026828029 scopus 로고
    • Proton gradient-driven import of the 16 kDa oxygen-evolving complex protein as the full precursor protein by isolated thylakoids
    • Klösgen RB, Brock IW, Herrmann RG, Robinson C. 1992. Proton gradient-driven import of the 16 kDa oxygen-evolving complex protein as the full precursor protein by isolated thylakoids. Plant Mol. Biol. 18:1031-34
    • (1992) Plant Mol. Biol. , vol.18 , pp. 1031-1034
    • Klösgen, R.B.1    Brock, I.W.2    Herrmann, R.G.3    Robinson, C.4
  • 70
    • 0027603071 scopus 로고
    • The primary structure of a cDNA for PsaN encoding an extrinsic lumenal polypeptide of barley photosystem I
    • Knoetzel J, Simpson DJ. 1993. The primary structure of a cDNA for PsaN encoding an extrinsic lumenal polypeptide of barley photosystem I. Plant Mol. Biol. 22:337-45
    • (1993) Plant Mol. Biol. , vol.22 , pp. 337-345
    • Knoetzel, J.1    Simpson, D.J.2
  • 71
    • 0028365045 scopus 로고
    • The SecA inhibitor, azide, reversibly blocks the translocation of a subset of proteins across the chloroplast thylakoid membrane
    • Knott TG, Robinson C. 1994. The SecA inhibitor, azide, reversibly blocks the translocation of a subset of proteins across the chloroplast thylakoid membrane. J. Biol. Chem. 269:7843-46
    • (1994) J. Biol. Chem. , vol.269 , pp. 7843-7846
    • Knott, T.G.1    Robinson, C.2
  • 72
    • 0026744686 scopus 로고
    • Isolation and characterization of a cDNA clone encoding a cognate 70-kDa heat shock protein of the chloroplast envelope
    • Ko K, Bornemisza O, Kourtz L, Ko ZW, Plaxton WC, Cashmore AR. 1992. Isolation and characterization of a cDNA clone encoding a cognate 70-kDa heat shock protein of the chloroplast envelope. J Biol. Chem. 267:2986-93
    • (1992) J Biol. Chem. , vol.267 , pp. 2986-2993
    • Ko, K.1    Bornemisza, O.2    Kourtz, L.3    Ko, Z.W.4    Plaxton, W.C.5    Cashmore, A.R.6
  • 73
    • 0028862147 scopus 로고
    • Isolation and characterization of a cDNA clone encoding a member of the Com44/Cim44 envelope components of the chloroplast protein import apparatus
    • Ko K, Budd D,Wu CB, Seibert F, Kourtz L, Ko ZW. 1995. Isolation and characterization of a cDNA clone encoding a member of the Com44/Cim44 envelope components of the chloroplast protein import apparatus. J. Biol. Chem. 270:28601-8
    • (1995) J. Biol. Chem. , vol.270 , pp. 28601-28608
    • Ko, K.1    Budd, D.2    Wu, C.B.3    Seibert, F.4    Kourtz, L.5    Ko, Z.W.6
  • 74
    • 0024422740 scopus 로고
    • Targeting of proteins to the thylakoid lumen by the bipartite transit peptide of the 33-kd oxygen-evolving protein
    • Ko K, Cashmore AR. 1989. Targeting of proteins to the thylakoid lumen by the bipartite transit peptide of the 33-kd oxygen-evolving protein. EMBO J. 8:3187-94
    • (1989) EMBO J. , vol.8 , pp. 3187-3194
    • Ko, K.1    Cashmore, A.R.2
  • 75
    • 0026750052 scopus 로고
    • Carboxyl-terminal sequences can influence the in vitro import and intraorganellar targeting of chloroplast protein precursors
    • Ko K, Ko ZW. 1992. Carboxyl-terminal sequences can influence the in vitro import and intraorganellar targeting of chloroplast protein precursors. J. Biol. Chem. 267:13910-16
    • (1992) J. Biol. Chem. , vol.267 , pp. 13910-13916
    • Ko, K.1    Ko, Z.W.2
  • 76
    • 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. 1993. 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. 34:315-19
    • (1993) Plant Cell Physiol. , vol.34 , pp. 315-319
    • Konishi, T.1    Watanabe, A.2
  • 77
    • 0029905725 scopus 로고    scopus 로고
    • Protein translocation at the envelope and thylakoid membranes of chloroplasts
    • Kouranov A, Schnell DJ. 1996. Protein translocation at the envelope and thylakoid membranes of chloroplasts. J. Biol. Chem. 271:31009-12
    • (1996) J. Biol. Chem. , vol.271 , pp. 31009-31012
    • Kouranov, A.1    Schnell, D.J.2
  • 78
    • 0031034588 scopus 로고    scopus 로고
    • The early stage of chloroplast protein import involves Com70
    • Kourtz L, Ko K. 1997. The early stage of chloroplast protein import involves Com70. J. Biol. Chem. 272:2808-13
    • (1997) J. Biol. Chem. , vol.272 , pp. 2808-2813
    • Kourtz, L.1    Ko, K.2
  • 80
    • 0024288942 scopus 로고
    • The chlorophyll a/b binding protein inserts into the thylakoids independent of its cognate transit peptide
    • Lamppa GK. 1988. The chlorophyll a/b binding protein inserts into the thylakoids independent of its cognate transit peptide. J. Biol. Chem. 263:14996-99
    • (1988) J. Biol. Chem. , vol.263 , pp. 14996-14999
    • Lamppa, G.K.1
  • 81
    • 0029041304 scopus 로고
    • A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes
    • Li XX, Henry R, Yuan JG, Cline K, Huffman NE. 1995. A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes. Proc. Natl. Acad. Sci. USA 92:3789-93
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3789-3793
    • Li, X.X.1    Henry, R.2    Yuan, J.G.3    Cline, K.4    Huffman, N.E.5
  • 84
    • 0029775088 scopus 로고    scopus 로고
    • Topology of IEP1 10, a component of the chloroplastic protein import machinery present in the inner envelope membrane
    • Lübeck J, Soll J, Akita M, Nielsen E, Keegstra K. 1996. Topology of IEP1 10, a component of the chloroplastic protein import machinery present in the inner envelope membrane. EMBO J. 15:4230-38
    • (1996) EMBO J. , vol.15 , pp. 4230-4238
    • Lübeck, J.1    Soll, J.2    Akita, M.3    Nielsen, E.4    Keegstra, K.5
  • 85
    • 0029894578 scopus 로고    scopus 로고
    • Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope
    • Ma YK, Kouranov A, LaSala SE, Schnell DJ. 1996. Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope. J. Cell Biol. 134:315-27
    • (1996) J. Cell Biol. , vol.134 , pp. 315-327
    • Ma, Y.K.1    Kouranov, A.2    Lasala, S.E.3    Schnell, D.J.4
  • 86
    • 0028239208 scopus 로고
    • The thylakoid-targeting domain of the chloroplast Rieske iron-sulfur protein is located in the N-terminal hydrophobic region of the mature protein
    • Madueño F, Bradshaw SA, Gray JC. 1994. The thylakoid-targeting domain of the chloroplast Rieske iron-sulfur protein is located in the N-terminal hydrophobic region of the mature protein. J. Biol. Chem. 269:17458-63
    • (1994) J. Biol. Chem. , vol.269 , pp. 17458-17463
    • Madueño, F.1    Bradshaw, S.A.2    Gray, J.C.3
  • 87
    • 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. 1994. Multiple mechanisms for the targeting of photosystem I subunits F, H, K, L, and N into and across the thylakoid membrane. J. Biol. Chem. 269:27303-9
    • (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
  • 88
    • 0028877047 scopus 로고
    • Sec-dependent thylakoid protein translocation: Delta pH requirement is dictated by passenger protein and ATP concentration
    • Mant A, Schmidt I, Herrmann RG, Robinson C, Klösgen RB. 1995. Sec-dependent thylakoid protein translocation: delta pH requirement is dictated by passenger protein and ATP concentration. J. Biol. Chem. 270:23275-81
    • (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
  • 91
    • 0026409326 scopus 로고
    • The full precursor of the 33-kDa oxygen-evolving complex protein of wheat is exported by Escherichia coli and processed to the mature size
    • Meadows JW, Robinson C. 1991. The full precursor of the 33-kDa oxygen-evolving complex protein of wheat is exported by Escherichia coli and processed to the mature size. Plant Mol. Biol. 17:1241-43
    • (1991) Plant Mol. Biol. , vol.17 , pp. 1241-1243
    • Meadows, J.W.1    Robinson, C.2
  • 92
    • 38249026275 scopus 로고
    • Targeting of a foreign protein into the thylakoid lumen of pea chloroplasts
    • Meadows JW, Shackleton JB, Hulford A, Robinson C. 1989. Targeting of a foreign protein into the thylakoid lumen of pea chloroplasts. FEBS Lett. 253:244-46
    • (1989) FEBS Lett. , vol.253 , pp. 244-246
    • Meadows, J.W.1    Shackleton, J.B.2    Hulford, A.3    Robinson, C.4
  • 94
    • 0027433308 scopus 로고
    • GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
    • Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P. 1993. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366:351-54
    • (1993) Nature , vol.366 , pp. 351-354
    • Miller, J.D.1    Wilhelm, H.2    Gierasch, L.3    Gilmore, R.4    Walter, P.5
  • 95
    • 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. 1991. A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J. Biol. Chem. 266:12189-93
    • (1991) J. Biol. Chem. , vol.266 , pp. 12189-12193
    • Mould, R.M.1    Robinson, C.2
  • 96
    • 0026050854 scopus 로고
    • Transport of proteins into chloroplasts: Requirements for the efficient import of two lumenal oxygen-evolving complex proteins into isolated thylakoids
    • Mould RM, Shackleton JB, 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. 266:17286-89
    • (1991) J. Biol Chem. , vol.266 , pp. 17286-17289
    • Mould, R.M.1    Shackleton, J.B.2    Robinson, C.3
  • 97
    • 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. 1994. Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J. Biol. Chem. 269:1338-41
    • (1994) J. Biol. Chem. , vol.269 , pp. 1338-1341
    • Nakai, M.1    Goto, A.2    Nohara, T.3    Sugita, D.4    Endo, T.5
  • 98
    • 0031048279 scopus 로고    scopus 로고
    • Stable association of chloroplastic precursors with protein-translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone
    • Nielsen E, Akita M, Davila-Aponte J, Keegstra K. 1997. Stable association of chloroplastic precursors with protein-translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone. EMBO J. 16:935-46
    • (1997) EMBO J. , vol.16 , pp. 935-946
    • Nielsen, E.1    Akita, M.2    Davila-Aponte, J.3    Keegstra, K.4
  • 99
    • 0028169710 scopus 로고
    • Import of barley photosystem I subunit N into the thylakoid lumen is mediated by a bipartite presequence lacking an intermediate processing site
    • Nielsen VS, Mant A, Knoetzel J, Møller BL, Robinson C. 1994. Import of barley photosystem I subunit N into the thylakoid lumen is mediated by a bipartite presequence lacking an intermediate processing site. J. Biol. Chem. 269:3762-66
    • (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
  • 100
    • 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. 1996. Cytochrome f encoded by the chloroplast genome is imported into thylakoids via the SecA-dependent pathway. Biochem. Biophys. Res. Commun. 224:474-78
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 474-478
    • Nohara, T.1    Asai, T.2    Nakai, M.3    Sugiura, M.4    Endo, T.5
  • 101
    • 0028998696 scopus 로고
    • Isolation and characterization of the cDNA for pea chloroplast SecA: Evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplasts
    • Nohara T, Nakai M, Goto A, Endo T. 1995. Isolation and characterization of the cDNA for pea chloroplast SecA: evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplasts. FEBS Lett. 364:305-8
    • (1995) FEBS Lett. , vol.364 , pp. 305-308
    • Nohara, T.1    Nakai, M.2    Goto, A.3    Endo, T.4
  • 102
    • 0026770791 scopus 로고
    • Precursor for the light-harvesting chlorophyll a/b-binding protein synthesized in Escherichia coli blocks import of the small subunit of ribulose-l,5-bisphosphate carboxylase/oxygenase
    • Oblong JE, Lamppa GK. 1992. Precursor for the light-harvesting chlorophyll a/b-binding protein synthesized in Escherichia coli blocks import of the small subunit of ribulose-l,5-bisphosphate carboxylase/oxygenase. J. Biol. Chem. 267:14328-34
    • (1992) J. Biol. Chem. , vol.267 , pp. 14328-14334
    • Oblong, J.E.1    Lamppa, G.K.2
  • 103
    • 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. 1990. Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc. Natl. Acad. Sci. USA 87:8227-31
    • (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
  • 104
    • 0026571378 scopus 로고
    • The binding of precursor proteins to chloroplasts requires nucleoside triphosphates in the intermembrane space
    • Olsen LJ, Keegstra K. 1992. The binding of precursor proteins to chloroplasts requires nucleoside triphosphates in the intermembrane space. J. Biol. Chem. 267:433-39
    • (1992) J. Biol. Chem. , vol.267 , pp. 433-439
    • Olsen, L.J.1    Keegstra, K.2
  • 105
    • 0024978251 scopus 로고
    • ATP is required for the binding of precursor proteins to chloroplasts
    • Olsen LJ, Theg SM, Selman BR, Keegstra K. 1989. ATP is required for the binding of precursor proteins to chloroplasts. J. Biol. Chem. 264:6724-29
    • (1989) J. Biol. Chem. , vol.264 , pp. 6724-6729
    • Olsen, L.J.1    Theg, S.M.2    Selman, B.R.3    Keegstra, K.4
  • 106
    • 0023336093 scopus 로고
    • Protein import in chloroplasts requires a chloroplast ATPase
    • Pain D, Blobel G. 1987. Protein import in chloroplasts requires a chloroplast ATPase. Proc. Natl. Acad. Sci. USA 84:3288-92
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3288-3292
    • Pain, D.1    Blobel, G.2
  • 107
    • 0026071203 scopus 로고
    • A stromal protein factor maintains the solubility and insertion competence of an imported thylakoid membrane protein
    • Payan LA, Cline K. 1991. A stromal protein factor maintains the solubility and insertion competence of an imported thylakoid membrane protein. J. Cell Biol. 112:603-13
    • (1991) J. Cell Biol. , vol.112 , pp. 603-613
    • Payan, L.A.1    Cline, K.2
  • 108
    • 0026075507 scopus 로고
    • Synthetic analogues of a transit peptide inhibit binding or translocation of chloroplastic precursor proteins
    • Perry SE, Buvinger WE, Bennett J, Keegstra K. 1991. Synthetic analogues of a transit peptide inhibit binding or translocation of chloroplastic precursor proteins. J. Biol. Chem. 266:11882-89
    • (1991) J. Biol. Chem. , vol.266 , pp. 11882-11889
    • Perry, S.E.1    Buvinger, W.E.2    Bennett, J.3    Keegstra, K.4
  • 109
    • 0027953126 scopus 로고
    • Envelope membrane proteins that interact with chloroplastic precursor proteins
    • Perry SE, Keegstra K. 1994. Envelope membrane proteins that interact with chloroplastic precursor proteins. Plant Cell 6:93-105
    • (1994) Plant Cell , vol.6 , pp. 93-105
    • Perry, S.E.1    Keegstra, K.2
  • 111
    • 0001343250 scopus 로고
    • A high-resolution gene map of the chloroplast genome of the red alga Porphyra purpurea
    • Reith M, Mulholland J. 1993. A high-resolution gene map of the chloroplast genome of the red alga Porphyra purpurea. Plant Cell 5:465
    • (1993) Plant Cell , vol.5 , pp. 465
    • Reith, M.1    Mulholland, J.2
  • 112
    • 0027980013 scopus 로고
    • The presequence of a chimeric construct dictates which of two mechanisms are utilized 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, et al. 1994. The presequence of a chimeric construct dictates which of two mechanisms are utilized for translocation across the thylakoid membrane: evidence for the existence of two distinct translocation systems. EMBO J. 13:279-85
    • (1994) EMBO J. , vol.13 , pp. 279-285
    • Robinson, C.1    Cai, D.2    Hulford, A.3    Brock, I.W.4    Michl, D.5
  • 113
    • 0021765413 scopus 로고
    • Transport of proteins into chloroplasts: Partial purification of a chloroplast protease involved in the processing of imported precursor polypeptides
    • Robinson C, Ellis RJ. 1984. Transport of proteins into chloroplasts: partial purification of a chloroplast protease involved in the processing of imported precursor polypeptides. Eur. J. Biochem. 142:337-42
    • (1984) Eur. J. Biochem. , vol.142 , pp. 337-342
    • Robinson, C.1    Ellis, R.J.2
  • 114
    • 0028519276 scopus 로고
    • Targeting of proteins into and across the thylakoid membrane-a multitude of mechanisms
    • Robinson C, Klösgen RB. 1994. Targeting of proteins into and across the thylakoid membrane-a multitude of mechanisms. Plant Mol. Biol. 26:15-24
    • (1994) Plant Mol. Biol. , vol.26 , pp. 15-24
    • Robinson, C.1    Klösgen, R.B.2
  • 116
    • 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 RA, Theg SM. 1996. 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. 111:1329-38
    • (1996) Plant Physiol. , vol.111 , pp. 1329-1338
    • Roffey, R.A.1    Theg, S.M.2
  • 117
  • 118
    • 0022366771 scopus 로고
    • Binding of pea cytochrome f to the inner membrane of Escherichia coli requires the bacterial secA gene product
    • Rothstein SJ, Gatenby AA, Willey DL, Gray JC. 1985. Binding of pea cytochrome f to the inner membrane of Escherichia coli requires the bacterial secA gene product. Proc. Natl. Acad. Sci. USA 82:7955-59
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7955-7959
    • Rothstein, S.J.1    Gatenby, A.A.2    Willey, D.L.3    Gray, J.C.4
  • 119
    • 0026713541 scopus 로고
    • Identification of a chloroplastencoded secA gene homologue in a chromophytic alga: Possible role in chloroplast protein translocation
    • Scaramuzzi CD, Miller RG, Stokes HW. 1992. Identification of a chloroplastencoded secA gene homologue in a chromophytic alga: possible role in chloroplast protein translocation. Curr. Genet. 22:421-27
    • (1992) Curr. Genet. , vol.22 , pp. 421-427
    • Scaramuzzi, C.D.1    Miller, R.G.2    Stokes, H.W.3
  • 120
    • 0026652939 scopus 로고
    • Characterization of a chloroplastencoded secY homologue and atpH from a chromophytic alga: Evidence for a novel chloroplast genome
    • Scaramuzzi CD, Stokes HW, Hiller RG. 1992. Characterization of a chloroplastencoded secY homologue and atpH from a chromophytic alga: evidence for a novel chloroplast genome. FEBS Lett. 304:119-23
    • (1992) FEBS Lett. , vol.304 , pp. 119-123
    • Scaramuzzi, C.D.1    Stokes, H.W.2    Hiller, R.G.3
  • 121
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G, Dobberstein B. 1996. Common principles of protein translocation across membranes. Science 271:1519-26
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 122
    • 0027469030 scopus 로고
    • Identification of intermediates in the pathway of protein import into chloroplasts and their localization to envelope contact sites
    • Schnell DJ, Blobel G. 1993. Identification of intermediates in the pathway of protein import into chloroplasts and their localization to envelope contact sites. J. Cell Biol. 120:103-15
    • (1993) J. Cell Biol. , vol.120 , pp. 103-115
    • Schnell, D.J.1    Blobel, G.2
  • 124
    • 0028109712 scopus 로고
    • Isolation of components of the chloroplast protein import machinery
    • Schnell DJ, Kessler F, Blobel G. 1994. Isolation of components of the chloroplast protein import machinery. Science 266:1007-12
    • (1994) Science , vol.266 , pp. 1007-1012
    • Schnell, D.J.1    Kessler, F.2    Blobel, G.3
  • 125
    • 0029257229 scopus 로고
    • A constituent of the chloroplast import complex represents a new type of GTP-binding protein
    • Seedorf M, Waegemann K, Soll J. 1995. A constituent of the chloroplast import complex represents a new type of GTP-binding protein. Plant J. 7:401-11
    • (1995) Plant J. , vol.7 , pp. 401-411
    • Seedorf, M.1    Waegemann, K.2    Soll, J.3
  • 126
    • 0025297347 scopus 로고
    • Expression in Escherichia coli of the psbO gene encoding the 33 kD protein of the oxygenevolving complex from spinach
    • Seidler A, Michel H. 1990. Expression in Escherichia coli of the psbO gene encoding the 33 kD protein of the oxygenevolving complex from spinach. EMBO J. 9:1743-48
    • (1990) EMBO J. , vol.9 , pp. 1743-1748
    • Seidler, A.1    Michel, H.2
  • 127
    • 0347307470 scopus 로고    scopus 로고
    • The maize gene Hcf106 encodes an ancient conserved protein required for Sec-independent protein translocation
    • In press
    • Settles M, Yonetani A, Baron A, Bush D, Cline K, Martienssen R. 1997. The maize gene Hcf106 encodes an ancient conserved protein required for Sec-independent protein translocation. Science. In press
    • (1997) Science
    • Settles, M.1    Yonetani, A.2    Baron, A.3    Bush, D.4    Cline, K.5    Martienssen, R.6
  • 128
    • 0025830411 scopus 로고
    • Transport of proteins into chloroplasts. the thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions
    • Shackleton JB, Robinson C. 1991. Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions. J. Biol. Chem. 266:12152-56
    • (1991) J. Biol. Chem. , vol.266 , pp. 12152-12156
    • Shackleton, J.B.1    Robinson, C.2
  • 129
    • 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. 1986. The role of the transit peptide in the routing of precursors toward different chloroplast compartments. Cell 46:365-75
    • (1986) Cell , vol.46 , pp. 365-375
    • Smeekens, S.1    Bauerle, C.2    Hageman, J.3    Keegstra, K.4    Weisbeek, P.5
  • 130
    • 0028284408 scopus 로고
    • Mutations in a signal sequence for the thylakoid membrane identify multiple protein transport pathways and nuclear suppressors
    • Smith TA, Kohorn BD. 1994. Mutations in a signal sequence for the thylakoid membrane identify multiple protein transport pathways and nuclear suppressors. J. Cell Biol. 126:365-74
    • (1994) J. Cell Biol. , vol.126 , pp. 365-374
    • Smith, T.A.1    Kohorn, B.D.2
  • 131
    • 0009867147 scopus 로고
    • The 20-kDa apo-polypeptide of the chlorophyll a/b protein complex CP24. Characterization and complete primary amino acid sequence
    • ed. M Bakscheffsky. The Hague: Kluwer
    • Spangfort M, Larsson UK, Ljungberg U, Ryberg M, Andersson B, et al. 1990. The 20-kDa apo-polypeptide of the chlorophyll a/b protein complex CP24. Characterization and complete primary amino acid sequence. In Current Research in Photosynthesis, ed. M Bakscheffsky, 2:253-56. The Hague: Kluwer
    • (1990) Current Research in Photosynthesis , vol.2 , pp. 253-256
    • Spangfort, M.1    Larsson, U.K.2    Ljungberg, U.3    Ryberg, M.4    Andersson, B.5
  • 132
    • 0023225548 scopus 로고
    • Nucleotide sequence of cDNA clones encoding the complete "33 kDa" precursor protein associated with the photosynthetic oxygen-evolving complex from spinach
    • Tagi A, Hermans J, Steppuhn J, Jansson C, Vater F, et al. 1987. Nucleotide sequence of cDNA clones encoding the complete "33 kDa" precursor protein associated with the photosynthetic oxygen-evolving complex from spinach. Mol. Gen. Genet. 207:288-93
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 288-293
    • Tagi, A.1    Hermans, J.2    Steppuhn, J.3    Jansson, C.4    Vater, F.5
  • 133
    • 0024978279 scopus 로고
    • Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes
    • Theg SM, Bauerle C, Olsen LJ, Selman BR, Keegstra K. 1989. Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes. J. Biol, Chem. 264:6730-36
    • (1989) J. Biol, Chem. , vol.264 , pp. 6730-6736
    • Theg, S.M.1    Bauerle, C.2    Olsen, L.J.3    Selman, B.R.4    Keegstra, K.5
  • 134
    • 0027298346 scopus 로고
    • Protein import into chloroplasts
    • Theg SM, Scott SV. 1993. Protein import into chloroplasts. Trends Cell Biol. 3:186-90
    • (1993) Trends Cell Biol. , vol.3 , pp. 186-190
    • Theg, S.M.1    Scott, S.V.2
  • 135
    • 0029053516 scopus 로고
    • A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway
    • Tranel PJ, Froehlich J, Goyal A, Keegstra K. 1995. A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway. EMBO J. 14:2436-46
    • (1995) EMBO J. , vol.14 , pp. 2436-2446
    • Tranel, P.J.1    Froehlich, J.2    Goyal, A.3    Keegstra, K.4
  • 136
    • 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. 1997. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88:187-96
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 137
    • 0027530587 scopus 로고
    • SecA is plastidencoded in a red alga: Implications for the evolution of plastid genomes and the thylakoid protein import apparatus
    • Valentin K. 1993. SecA is plastidencoded in a red alga: implications for the evolution of plastid genomes and the thylakoid protein import apparatus. Mol. Gen. Genet. 236:245-50
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 245-250
    • Valentin, K.1
  • 138
    • 0347937661 scopus 로고
    • The transit peptide of a chlorophyll a/b-binding protein is not sufficient to insert neomycin phosphotransferase II in the thylakoid membrane
    • Van Den Broeck G, Van Houtven A, Van Montague M, Herrera-Estrella L. 1988. The transit peptide of a chlorophyll a/b-binding protein is not sufficient to insert neomycin phosphotransferase II in the thylakoid membrane. Plant Sci. 58: 171-76
    • (1988) Plant Sci. , vol.58 , pp. 171-176
    • Van Den Broeck, G.1    Van Houtven, A.2    Van Montague, M.3    Herrera-Estrella, L.4
  • 139
    • 0345611654 scopus 로고
    • A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases
    • VanderVere PS, Bennett TM, Oblong JE, Lamppa GK. 1995. 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 92:7177-81
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7177-7181
    • Vandervere, P.S.1    Bennett, T.M.2    Oblong, J.E.3    Lamppa, G.K.4
  • 140
    • 0028981693 scopus 로고
    • Evidence for SecA- And delta pH-independent insertion of D1 into thylakoids
    • Van Wijk K, Knott TG, Robinson C. 1995. Evidence for SecA- and delta pH-independent insertion of D1 into thylakoids. FEBS Lett. 368:263-66
    • (1995) FEBS Lett. , vol.368 , pp. 263-266
    • Van Wijk, K.1    Knott, T.G.2    Robinson, C.3
  • 141
    • 0024288943 scopus 로고
    • What is the role of the transit peptide in thylakoid integration of the light-harvesting chloroplyll a/b protein
    • Viitanen PV, Doran ER, Dunsmuir P. 1988. What is the role of the transit peptide in thylakoid integration of the light-harvesting chloroplyll a/b protein. J. Biol. Chem. 263:15000-7
    • (1988) J. Biol. Chem. , vol.263 , pp. 15000-15007
    • Viitanen, P.V.1    Doran, E.R.2    Dunsmuir, P.3
  • 142
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker R, Barkan A. 1995. Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J. 14:3905-14
    • (1995) EMBO J. , vol.14 , pp. 3905-3914
    • Voelker, R.1    Barkan, A.2
  • 143
    • 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. 1997. Transposon-disruption of a maize nuclear gene, tha1, encoding a chloroplast SecA homologue: in vivo role of cp-SecA in thylakoid protein targeting. Genetics 145:467-78
    • (1997) Genetics , vol.145 , pp. 467-478
    • Voelker, R.1    Mendel-Hartvig, J.2    Barkan, A.3
  • 144
    • 0021856417 scopus 로고
    • Signal sequences: The limits of variation
    • Von Heijne G. 1985. Signal sequences: the limits of variation. J. Mol. Biol 184:99-105
    • (1985) J. Mol. Biol , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 145
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • Von Heijne G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-90
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 146
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • Von Heijne G, Steppuhn J, Herrmann RG. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180:535-45
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 147
    • 0025093379 scopus 로고
    • Translocation of proteins into isolated chloroplasts requires cytosolic factors to obtain import competence
    • Waegemann K, Paulsen H, Soll J. 1990. Translocation of proteins into isolated chloroplasts requires cytosolic factors to obtain import competence. FEBS Lett. 261:89-92
    • (1990) FEBS Lett. , vol.261 , pp. 89-92
    • Waegemann, K.1    Paulsen, H.2    Soll, J.3
  • 148
    • 0000489161 scopus 로고
    • Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts
    • Waegemann K, Soll J. 1991. Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts. Plant J. 1:149-58
    • (1991) Plant J. , vol.1 , pp. 149-158
    • Waegemann, K.1    Soll, J.2
  • 149
    • 0024769462 scopus 로고
    • Characterization of cDNA clones encoding the extrinsic 23 kDa polypeptide of the oxygen-evolving complex of photosystem II in pea
    • Wales R, Newman BJ, Rose SA, Pappin D, Gray JC. 1989. Characterization of cDNA clones encoding the extrinsic 23 kDa polypeptide of the oxygen-evolving complex of photosystem II in pea. Plant Mol. Biol. 13:573-82
    • (1989) Plant Mol. Biol. , vol.13 , pp. 573-582
    • Wales, R.1    Newman, B.J.2    Rose, S.A.3    Pappin, D.4    Gray, J.C.5
  • 150
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter P, Johnson AE. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10:87-119
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 151
    • 0029909480 scopus 로고    scopus 로고
    • Escherichia coli preprotein translocase
    • Wickner W, Leonard MR. 1996. Escherichia coli preprotein translocase. J. Biol. Chem. 271:29514-16
    • (1996) J. Biol. Chem. , vol.271 , pp. 29514-29516
    • Wickner, W.1    Leonard, M.R.2
  • 152
    • 0028595688 scopus 로고
    • Identification of chloroplast envelope proteins in close proximity to a partially translocated chimeric precursor protein
    • Wu CB, Seibert FS, Ko K. 1994. Identification of chloroplast envelope proteins in close proximity to a partially translocated chimeric precursor protein. J. Biol. Chem. 269:32264-71
    • (1994) J. Biol. Chem. , vol.269 , pp. 32264-32271
    • Wu, C.B.1    Seibert, F.S.2    Ko, K.3
  • 153
    • 0026635621 scopus 로고
    • Involvement of a chloroplast HSP70 heat shock protein in the integration of a protein (light-harvesting complex protein precursor) into the thylakoid membrane
    • Yalovsky S, Paulsen H, Michaeli D, Chitnis PR, Nechushtai R. 1992. Involvement of a chloroplast HSP70 heat shock protein in the integration of a protein (light-harvesting complex protein precursor) into the thylakoid membrane. Proc. Natl. Acad. Sci. USA 89:5616-19
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5616-5619
    • Yalovsky, S.1    Paulsen, H.2    Michaeli, D.3    Chitnis, P.R.4    Nechushtai, R.5
  • 154
    • 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 JG, Cline K. 1994. 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. 269:18463-67
    • (1994) J. Biol. Chem. , vol.269 , pp. 18463-18467
    • Yuan, J.G.1    Cline, K.2
  • 155
    • 0027260665 scopus 로고
    • Stromal factor plays an essential role in protein integration into thylakoids that cannot be replaced by unfolding or by heat shock protein Hsp70
    • Yuan JG, Henry R, Cline K. 1993. Stromal factor plays an essential role in protein integration into thylakoids that cannot be replaced by unfolding or by heat shock protein Hsp70. Proc. Natl. Acad. Sci. USA 90:8552-56
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8552-8556
    • Yuan, J.G.1    Henry, R.2    Cline, K.3
  • 156
    • 0027961026 scopus 로고
    • SecA homolog in protein transport within chloroplasts: Evidence for endosymbiont-derived sorting
    • Yuan JG, Henry R, McCaffery M, Cline K. 1994. SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting. Science 266:796-98
    • (1994) Science , vol.266 , pp. 796-798
    • Yuan, J.G.1    Henry, R.2    McCaffery, M.3    Cline, K.4
  • 157
    • 0030976679 scopus 로고    scopus 로고
    • On the mode of integration of plastidencoded components of the cytochrome bf complex into thylakoid membranes
    • Zak E, Sokolenko A, Unterholzner G, Altschmied L, Herrmann RG. 1997. On the mode of integration of plastidencoded components of the cytochrome bf complex into thylakoid membranes. Planta 201:334-41
    • (1997) Planta , vol.201 , pp. 334-341
    • Zak, E.1    Sokolenko, A.2    Unterholzner, G.3    Altschmied, L.4    Herrmann, R.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.