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1998 | 20 | 4 |

Tytuł artykułu

Targeting of proteins into and within the chloroplast

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN

Słowa kluczowe

Wydawca

-

Rocznik

Tom

20

Numer

4

Opis fizyczny

p.437-451,fig.

Twórcy

  • University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland

Bibliografia

  • Akita M., Nielsen E., Keegstra K. 1997. Identification of protein transport complex in the chloroplastic envelope membrane via chemical cross-linking. J. Cell Biol., 136: 983–994.
  • America T., Hageman J., Guera A., Rook F., Archer K., Keegstra K., Weisbeek P. 1994. Methotrexate does not block import of a DHFR fusion protein into chloroplast. Plant Mol. Biol., 24: 283–294.
  • Berghöfer J., Karnauchov I., Herrmann R.G., Klösgen R.B. 1995. Isolation and characterization of cDNA encoding the SecA protein from spinach chloroplast: evidence for azide-resistance of Sec-dependent protein translocation across thylakoid membranes of spinach. J. Biol. Chem., 270: 18341–18346.
  • Bogsch E., Brink S., Robinson C. 1997. 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: 3851–3859.
  • Brink S., Fischer K., Klösgen R.B., Flügge U-I. 1995. Sorting of nuclear-encoded chloroplast membrane proteins to the envelope and the thylakoid membrane. J. Biol. Chem., 270: 20808–20815.
  • Bruce B.D., Keegstra K. 1994. Translocation of proteins across chloroplast membrane. Advance in Molecular and Cell Biology, 10: 389–430.
  • Buvinger W.E., Michel H., Bennett J. 1989. A truncated analog of a pre-light-harvesting chlorophyll a/b protein II transit peptide inhibits protein import into chloroplast. J. Biol. Chem., 264: 1195–1202.
  • Chaddock A.M., Mant A., Karnauchov I., Brink S., Herrmann R.G., Klsgen R.B., Robinson C. 1995. A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the pH-dependent thylakoidal protein translocase. EMBO J., 14: 2715–2722.
  • Chen D., Schnell D.J. 1997. Insertion of the 34-kDa chloroplast protein import component, IAP34, into the chloroplast outer membrane is dependent on its intrinsic GTP-binding capacity. J. Biol. Chem., 272: 6614–6620.
  • Chua N-H., Schmidt G.W. 1978. Post-translational transport into intact chloroplast of a precursor to the small subunit of ribulose-1,5-bisphosphatecarboxylase. Proc. Natl. Acad. Sci., USA 75: 6110–6114.
  • Chupin V., van’t Hoff R., Kruijff B. 1994. The transit sequence of a chloroplast precursor protein reorients the lipids in monogalactosyl diglyceride containing bilayers. FEBS Lett., 350: 104–108.
  • Clark S.A., Theg S.M. 1997. A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol. Biol. Cell, 8: 923–934.
  • Clausmeyer S., Klösgen R.B., Herrmann R.G. 1993. 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.
  • Cline K., Werner-Washburne M., Lubben T., Keegstra K. 1985. Precursor to two nuclear-encoded chloroplast protein bind to the outer envelope before being imported into chloroplast. J. Biol. Chem., 260: 3691–3696.
  • Cline K., Ettinger W.F., Theg S.M. 1992. Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence ATP. J. Biol. Chem., 267: 2688–2696.
  • Cline K., Henry R., Li C., Yuan J. 1993. Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J., 12: 4105–4114.
  • Cline K., Henry R. 1996. Import and routing of nucleus-encoded chloroplast proteins. Annu. Rev. Cell Dev. Biol., 12: 1–26.
  • Creighton A.M., Hulford A., Mant A., Robinson D., Robinson C. 1995. A monomeric, tightly folded stromal intermediate on the pH-dependent thylakoid protein import pathway. J. Biol. Chem., 270: 1663–1669.
  • de Boer A.D., Weisbeek P.J. 1991. Chloroplast protein topogenesis: import, sorting and assembly. Biochem. Biophys. Acta., 1071: 221–253.
  • de Castro Silva-Filho M., Wieers M-CH., Flügge U-I., Chaumont F., Boutry M. 1997. Different in vivo and in vitro targeting properties of the transit peptide of a chloroplast envelope inner membrane protein. J. Biol. Chem., 272: 15264–15269.
  • della Cioppa G., Kishore G.M. 1988. Import of precursor protein into chloroplasts is inhibited by the herbicide glyphosate. EMBO J., 7: 1299–1305.
  • Dreses-Werringloer U., Fischer K., Wachter E., Link T.A., Flügge U-I. 1991. cDNA sequence and deduced amino acid sequence of the precursor of the 37-kDa inner envelope membrane polypeptide from spinach chloroplasts. Its transit peptide contains an amphiphilic α-helix as the only detectable structural element. Eur. J. Biochem., 195: 361–368.
  • Eilers M., Schatz G. 1986. Binding of specific ligand inhibits import of a purified precursor protein into mitochondria. Nature, 322: 228–232.
  • Endo T., Kawamura K., Goto 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: 403–409.
  • Endo T., Kawamura K., Nakai M. 1992. The chloroplast-targeting domain od plastocyanin transit peptide can form a helical structure but does not have a high affinity for lipid bilayers. Eur. J. Biochem., 207: 671–675.
  • Fischer K., Weber A., Arbinger B., Brink S., Eckerskorn Ch., Flügge U-I. 1994. The 24 kDa outer envelope membrane protein from spinach chloroplast: molecular cloning, in vivo expression and import pathway of protein with unusual properties. Plant Mol. Biol., 25: 167–177.
  • Flügge U-I., Fischer K., Gross A., Sebald W., Lottspeich F., Eckerskorn C. 1989. The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplast: Nucleotide sequence of a full length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts. EMBO J., 8: 39–46.
  • Franklin A.E., Hoffman N.E. 1993. Characterization of a chloroplast homologue of the 54-kDa subunit of the signal recognition particle. J. Biol. Chem., 268: 22175–22180.
  • Friedman A.L., Keegstra K. 1989. Chloroplast protein import. Quantitative analysis of preursor binding. Plant Physiol., 89: 993–999.
  • Froehlich E.J., Keegstra K. 1997. Identification of a translocation intermediate occupaying functional protein import sites in the chloroplastic envelope membrane. J. Biol. Chem., 272: 8077–8082.
  • Fuks B., Schnell D.J. 1997. Mechanism of protein transport across the chloroplast envelope. Plant Physiol., 114: 405–410.
  • Gray J.C., Row P.E. 1995. Protein translocation across envelope membranes. Trends Cell Biol., 5: 243–247.
  • Guera A., America T., Van Waas M., Weisbeek P.J. 1993. A strong protein unfolding activity is associated with the binding of precursor chloroplast proteins to chloroplast envelopes. Plant Mol. Biol., 23: 309–324.
  • Hageman J., Robinson C., Smeekens S., Weisbeek P. 1986. A thylakoid processing protease is required for complete maturation of the lumen protein plastocyanin. Nature, 324: 567–569.
  • Haward S.R., Napier J.A., Gray J.C. 1997. Chloroplast Sec A functions as a membrane-associated component of the Sec-like protein translocase of pea chloroplast. Eur. J. Biochem., 248: 724–730.
  • 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: 10189–10192.
  • Henry R., Carrigan M., McCaffery M., Ma X., Cline K. 1997. 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.
  • Hirsch S., Muckel E., Heemeyer F., von Heijne G., Soll J. 1994. A receptor component of the chloroplast protein translocation machinery. Science, 266: 1989–1992.
  • Hoffman N.E., Franklin A.E., 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.
  • Horniak L., Pilon M., van’t Hoff R., Kruijff B. 1993. The secondary structure of the ferredoxin transit sequence is modulated by its interaction with negatively charged lipids. FEBS Lett., 334: 241–246.
  • James H.E., Bartling D., Musgrove J.E., Kirwin P.M., Herrmann R.G., Robinson C. 1989. Transport of proteins into chloroplast: 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.
  • Kapazoglou A., Sagliocco F., Dure L. 1995. PSII-T, a new nuclear encoded lumenal protein from photosystem II. J. Biol. Chem., 270: 12197–12202.
  • Karnauchov I., Cai D., Schmidt I., Herrmann R.G., Klösgen R.B. 1994. The thylakoid translocation of subunit 3 of photosystem I, the psaF gene product, depends on bipartite transit peptide and proceeds along an azide-sensitive pathway. J. Biol. Chem., 269: 32871–32878.
  • Keegstra K. 1989. Transport and routing of proteins into chloroplast. Cell, 56: 247–253.
  • Kessler F., Blobel G. 1996. Interaction of the protein import and folding machineries in chloroplast. Proc. Natl. Acad. Sci. USA, 93: 7684–7689.
  • Kessler F., Blobel G., Patel H.A., Schnell D.J. 1994. Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science, 266: 1035–1039.
  • Kim S.J., Robinson D., Robinson C. 1996. An Arabidopsis thaliana cDNA encoding PSII-X, a 4.1 kDa component of photosystem II: a bipartite presequence mediates SecA/pH-independent targeting into thylakoids. FEBS Lett., 390: 175–178.
  • Kim S.J., Robinson C., Mant A. 1998. Sec/SRP-independent insertion of two thylakoid membrane proteins bearing cleavable signal peptides. FEBS Lett., 424: 105–108.
  • Klösgen R.B. 1997. Protein transport into and across the thylakoid membrane. J. Photochem. Photobiol., 38: 1–9.
  • Klösgen R.B., Brock I.W., Herrmann R.G., 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: 1031–1034.
  • Kourtz K., Ko K. 1997. The early stage of chloroplast protein import involves Com 70. J. Biol. Chem., 272: 2808–2813.
  • Kuhn A., 1995. Major coat proteins of bacteriophage pf3 and M13 as model systems for Sec-independent protein transport. FEMS Microbiol. Rev., 17: 185–190.
  • Laidler V., Chaddock A.M., Knott R.F., Walker D., Robinson C., 1995. A SecY homologi in Arabidopsis thaliana: sequence of a full-length cDNA clone and import of the precursor protein into chloroplasts. J. Biol. Chem., 270: 17664–17667.
  • Lamppa K.G. 1988. The chlorophyll a/b-binding protein inserts into the thylakoids independent of its cognate transit peptide. J. Biol. Chem., 263: 14996–14999.
  • Lancelin J-M., Bally I., Arlaud G.J., Blackledge M., Gans P., Stein M., Jacquot J-P. 1994. NMR structure of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Lett., 343: 261–266.
  • Li X., Henry R., Yuan J., Cline K., Hoffman N.E. 1995. A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membrane. Proc. Natl. Acad. Sci., USA 92: 3789–3793.
  • Li H.M., Chen L.J. 1996. Protein targeting and integration signal for the chloroplastic outer envelope membrane. Plant Cell, 8: 2117–2126.
  • Li H.M., Chen L.J. 1997. A novel chloroplastic outer membrane-targeting signal that functions at both termini of passenger polypeptides. J. Biol. Chem., 272: 10968–10974.
  • Li H.M., More T., Keegstra K. 1991. Targeting of proteins to the outer envelope membrane uses a different pathway than transport into chloroplast. Plant Cell, 3: 709–717.
  • Li H.M., Sullivan T.D., Keegstra K. 1992. Information for targeting to the chloroplastic inner envelope membrane is contained in the mature region of the maize Bt1-encoded protein. J. Biol. Chem., 267: 18999–19004.
  • Lorković Z.J., Schrö W.P., Pakrasi H.B., Irrgang K.-D., Herrmann R.G., Oelmüller R. 1995. Molecular characterization of PsbW, a nuclear-encoded component of the photosystem II reaction center complex in spinach. Proc. Natl. Acad. Sci., 92: 8930–8934.
  • Lubeck L., Soll J., Akita M., Nielsen E., Keegstra K. 1996. Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane. EMBO J., 15: 4230–4238.
  • Ma Y., Kouranov A., LaSala S., Schnell D.J. 1996. Two components of the chlorplast protein import apparatus, IAP 86 and IAP 75 interact with the transit sequence during the recognition and translocation of precursor protein at the outer envelope. J. Cell. Biol., 134: 315–327.
  • Michl D., Robinson C., Shackelton J.B., Hermmann R.G., Klösgen R.B. 1994. Targeting of protein to the thylakoids by bipartite presequences: Cfoll is imported by a novel, third pathway. EMBO J., 13: 1310–1317.
  • Mould R.M., Robinson C. 1991. A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J. Biol. Chem., 266: 12189–12193.
  • Mould R.M., Knight J.S., Bogsch E., Gray J.C. 1997. Azide-sensitive thylakoid membrane insertion of chimeric cytochrome f polypeptides imported by isolated pea chloroplast. Plant J., 11: 1051–1058.
  • Muckel E., Soll J. 1996. A protein import receptor is inserted into the outer envelope membrane by a novel pathway. J. Biol. Chem., 271: 23846–23852.
  • Nielsen E., Akita M., Davila-Aponte J., Keegstra K. 1997. Stable association of chloroplastic precursor with protein-translocation complex that contain proteins from both envelope membranes and a stromal Hsp 100 molecular chaperone. EMBO J., 16: 935–946.
  • Nielsen V.S., Mant A., Knoetzel J., Lindberg Moller B., Robinson C. 1994. Import of barley photosystem I subunit N into the thylakoid lumen is mediated by bipartite presequence lacking an intermediate cleavage site: role of the delta pH in translocation across the thylakoid membrane. J. Biol. Chem., 269: 3762–3766.
  • Nohara T., Nakai M., Goto A., Endo T. 1995. Isolation and characterisation of the cDNA for pea chloroplast SecA. Evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplast. FEBS Lett., 364: 305–308.
  • Oblong J.E., Lamppa G.K. 1992. Precursor for the light-harvesting chlorophyll a/b-binding protein synthesised in Escherichia coli blocks import of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. J. Biol. Chem., 267: 14328–14334.
  • Oliver D.B., Cabelli R.J., Dolan K.M., Jarosik G.P. 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: 8227–8231.
  • Olsen L.J., Theg S.M., Selman B.R., Keegstra K. 1989. ATP is required for binding of precursor proteins to chloroplasts. J. Biol. Chem., 264: 6724–6729.
  • Pain D., Blobel G. 1987. Protein import into chloroplasts requires a chloroplast ATPase. Proc. Natl. Acad. Sci. USA, 84: 3288–3292.
  • Payan L.A., Cline K. 1991. A stromal protein factor maintains the solubility and insertion competence of an imported thylakoid membrane protein. J. Cell Biol., 112: 603–613.
  • Perry S.E., Buvinger W.E., Bennet J., Keegstra K. 1991. Synthetic analogues of a transit peptide inhibit binding or translocation of chloroplastic precursor protein. J. Biol. Chem., 266: 11882–11889.
  • Perry S.E., Keegstra K. 1994. Envelope membrane proteins that interact with chloroplastic precursor protein. Plant Cell, 6: 93–105.
  • Pfisterer J., Lachmann P., Kloppstech K. 1982. Transport of proteins into chloroplasts. Binding of nuclear-coded chloroplast protein to the chloroplast envelope. Eur. J. Biochem., 126: 143–148.
  • Pilon M., de Bower A.D., Knols L.S., Koppelman M., van der Graaf R.M., de Kruijff B., Weisbeek P.J. 1990. Expression in E. coli and purification of a translocation-competent precursor of the chloroplast protein ferredoxin. J. Biol. Chem., 265: 3358–3361.
  • Pilon M., Kruijff B., Weisbeek P.J. 1992. New insights into the import mechanism of the ferredoxin precursor into chloroplasts. J. Biol. Chem., 267:2548–2556.
  • Pilon M., Rietveld A.G., Weisbeek P.J., Kruijff B. 1992. Secondary structure and folding of a functional chloroplast precursor protein. J. Biol. Chem., 267: 19907–19913.
  • Robinson C., Mant A. 1997. Targeting of protein into and across the thylakoid membrane. T I P S, 11: 431–437.
  • Robinson C., Cai D., Hulford A., Brock I.W., Michl D., Hazell L., Schmidt I., Herrmann R.G., Klösgen R.B. 1994. The presequence of a chimeric construct dictates which of two mechanisms are utilised for translocation across the thylakoid membrane: evidence for the existence of two translocation systems. EMBO J., 13: 279–285.
  • Robinson C., Ellis R.J. 1984. Transport of protein into chloroplast: Partial purification of a chloroplast protease involved in the processing of imported precursor polypeptide. Eur. J. Biochem., 142: 337–342.
  • Robinson C., Klösgen R.B. 1994. Targeting of protein into and across the thylakoid membrane — a multitude of mechanisms. Plant Molec.Biol., 26: 15–24.
  • Robinson D., Karnauchov I., Herrmann R.G., Klösgen R.B., Robinson C. 1996. Protease-sensitive thylakoid import machinery for SecA-, ΔpH- and signal recognition particle-dependent protein targeting pathways, but not for CF0-II integration. Plant J., 10: 149–155.
  • Rothen R., Thiess M., Schumann P., Boschetti A. 1996. Import inhibition of poly(His) containing chloroplast precursor proteins by Ni2+ ions. FEBS Lett., 396: 135–138.
  • Salomon M., Fischer K., Flügge U-I., Soll J. 1990. Sequence analysis and protein import studies of an outer chloroplast envelope polypeptide. Proc.Natl.Acad.Sci. USA, 87: 5778–5782.
  • Salvucci M.E., Drake R.R., Broadbent K.P., Haley B.E., Hanson K.R., Mchale N.A. 1990. Plant Physiol., 93: 105–109.
  • Schnell D.J. 1995. Shedding light on the chloroplast protein import machinery. Cell, 83: 521–524.
  • Schnell D.J., Blobel G. 1993. Identification of intermediates in the pathway of protein import into chloroplast and their localization to envelope contact sites. J. Cell Biol., 120: 103–115.
  • Schnell D.J., Blobel G., Pain D. 1991. Signal peptide analogs derived from two chloroplast precursors interact with the signal recognition system of the chloroplast envelope. J. Biol. Chem., 266: 3335–3342.
  • Schnell D.J., Kessler F., Blobel G. 1994. Isolation of components of the chloroplast protein import machinery. Science, 266: 1007–1012.
  • Schreier P.H., Seftor E.A., Schnell J., Bohnert H.J. 1985. The use of nuclear encoded sequences to direct the light regulated synthesis and transport of a foreign protein into plant chloroplast. EMBO J., 4: 25–32.
  • Scott S.V., Theg S.M. 1996. A new chloroplast protein import intermediate reveals disting translocation machineries in the two envelope membranes: energetic and mechanistic implications. J. Cell Biol., 132: 63–75.
  • 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: 401–411.
  • Settles M., Yonetani A., Baron A., Bush D.R., Cline K., Martienssen R. 1997. Sec-Independent protein translocation by the maize Hcf106 protein. Science, 278: 1467–1470.
  • Smeekens S., Geerts D., Bauerle C., Weisbeek P. 1989. Essential function in chloroplast recognition of the ferredoxin transit peptide processing region. Mol. Gen. Genet., 216: 178–182.
  • Soll J. 1995. New insights into the protein import machinery of the chloroplasts outer envelope. Bot. Acta., 108: 277–282.
  • Sugita M., Sugiura M. 1996. Regulation of gene expression in chloroplasts of higher plants. Plant Mol. Biol., 32: 315–326.
  • Sugiura M. 1996. Structure and replication of chloroplast DNA. In: Frontiers in Molecular Biology: Molecular biology of Photosynthesis, eds. by Anderson, B. Salter, A.H. Barber, J. IRL Press: 58–74.
  • Theg S.M., Bauerle C., Olsen L.J., Selman B.R., Keegstra K. 1989. Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membrane. J. Biol. Chem., 264: 6730–6736.
  • Theg S.M., Scott S.V. 1993. Protein import into chloroplast. Trend. Cell Biol., 3:186–190.
  • Tranel P.J., 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: 2436–2446.
  • Tranel P.J., Keegstra K. 1996. A novel, bipartite transit peptide targets OEP75 to the outer membrane of chloroplast envelope. Plant Cell, 8: 2093–2104.
  • Van den Broeck G., Timko M.P., Kausch A.P., Cashmore A.R., van Montagu M., Herrera-Estrella L. 1985. Targeting of foreign protein to chloroplast by fusion to the transit peptide from the small subunit of ribulose 1,5-bisphosphate carboxylase. Nature, 313: 6110–6114.
  • van’t Hoff R., Kruijff B. 1995. Characterization of the import process of a transit peptide into chloroplast. J. Biol. Chem., 270: 22368–22373.
  • van’t Hoff R., van Klompenburg W., Pilon M., Kozubek A., de Korte-Kool G., Demel R.A., Weisbeek P.J., Kruijff B. 1993. The transit sequence mediates the specific interaction of the precursor of ferredoxin with chloroplast envelope membrane lipids. J. Biol. Chem., 268: 4037–4042.
  • Viitanen P.V., Doran E.R., Dunsmuir P. 1988. 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.
  • Voelker R., Barkan A. 1995. Two nuclear mutation disrupt distinct pathway for targeting to the chloroplast thylakiod. EMBO J., 14: 3905–3914.
  • 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: 467–478.
  • Vogel H., Fischer S., Valentin K. 1996. A model for the evolution of the plastid sec apparatus inferred from secY gene phylogeny. Plant Mol. Biol., 32: 685–692.
  • von Heijne G., Hirai T, Klösgen R.B., Steppuhn J., Bruce B.D., Keegstra K., Herrmann R.G. 1991. CHLPEP: A database of chloroplast transit peptides. Plant Mol. Biol. Rep., 9: 104–126.
  • von Heijne G., Nishikawa K. 1991. Chloroplast transit peptides: The perfect random coil. FEBS Lett, 278: 1–3.
  • von Heijne G., Steppuhn J., Herrmann R.G. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur J. Biochem., 180: 535–545.
  • Wagemann K., Paulsen H., Soll J. 1990. Translocation of proteins into isolated chloroplast require cytosolic factor to obtain import competence. FEBS Lett., 261: 89–92.
  • Waegemann K., Soll J. 1991. Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts. Plant. J., 1: 149–158.
  • Walker D., Chaddock A.M., Chaddock J.A., Roberts L.M., Lord J.M., Robinson C. 1996. Ricin a chain fused to a chloroplast-targeting signal is unfolded on the chloroplast surface prior to import across the envelope membranes. J. Biol. Chem., 271: 4082–4085.
  • Walter P., Johnson A.E. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol., 10: 87–119.
  • Wu C., Seibert F.S., Ko K. 1994. Identification of chloroplast envelope proteins in close proximity to a partially translocated chimeric precursor protein. J. Biol. Chem., 269: 32264–32271.
  • Yuan J., 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: 18463–18467.
  • Yuan J., 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: 8552–8556.
  • Yuan J., Henry R., McCaffery M., Cline K. 1994. SecA homolog in protein transport within chloroplast: evidence for endosymbiont-derived sorting. Science, 266: 796–798.

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