메뉴 건너뛰기




Volumn 2, Issue 6, 1999, Pages 513-519

Endosymbiosis and evolution of the plant cell

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0033485273     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(99)00025-4     Document Type: Review
Times cited : (128)

References (65)
  • 1
    • 0001204463 scopus 로고
    • Über Natur und Ursprung der Chromatophoren im Pflanzenreiche
    • [Title translation: On the origin of plastids in plants.]
    • Mereschkowsky C. Über Natur und Ursprung der Chromatophoren im Pflanzenreiche. Biol Zentralbl. 25:1905;593-604. [Title translation: On the origin of plastids in plants.].
    • (1905) Biol Zentralbl , vol.25 , pp. 593-604
    • Mereschkowsky, C.1
  • 2
    • 0000731173 scopus 로고
    • Bot Zeitung [Title translation: On the development of chloroplasts and chromoplasts.]
    • Schimper AFW: Uber die entwicklung der chlorophyllkörner und farbkörper, Bot Zeitung 1883, 41:105-114. [Title translation: On the development of chloroplasts and chromoplasts.].
    • (1883) Uber Die Entwicklung der Chlorophyllkörner und Farbkörper , vol.41 , pp. 105-114
    • Schimper, A.F.W.1
  • 3
    • 0032725631 scopus 로고    scopus 로고
    • Plastid division and development
    • A review of plastid division in plants.
    • Pyke K.A. Plastid division and development. Plant Cell. 11:1999;549-556. A review of plastid division in plants.
    • (1999) Plant Cell , vol.11 , pp. 549-556
    • Pyke, K.A.1
  • 4
    • 0032293815 scopus 로고    scopus 로고
    • Plastid division: The origin of replication
    • Pyke K.A. Plastid division: the origin of replication. Plant Cell. 10:1998;1971-1972.
    • (1998) Plant Cell , vol.10 , pp. 1971-1972
    • Pyke, K.A.1
  • 5
    • 0029149042 scopus 로고
    • Conserved cell and organelle division
    • Osteryoung K.W., Vierling E. Conserved cell and organelle division. Nature. 376:1995;473-474.
    • (1995) Nature , vol.376 , pp. 473-474
    • Osteryoung, K.W.1    Vierling, E.2
  • 6
    • 0032287069 scopus 로고    scopus 로고
    • Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial ftsZ
    • Analysis of ftsZ function using transgenics in Arabidopsis. The first identification of ftsZ genes whose products may function in the eukaryotic cytoplasm.
    • Osteryoung K.W., Stokes K.D., Rutherford S.M., Percival A.L., Lee W.Y. Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial ftsZ. Plant Cell. 10:1998;1991-2004. Analysis of ftsZ function using transgenics in Arabidopsis. The first identification of ftsZ genes whose products may function in the eukaryotic cytoplasm.
    • (1998) Plant Cell , vol.10 , pp. 1991-2004
    • Osteryoung, K.W.1    Stokes, K.D.2    Rutherford, S.M.3    Percival, A.L.4    Lee, W.Y.5
  • 7
    • 0032240930 scopus 로고    scopus 로고
    • Plastid division: Evidence for a prokaryotically derived mechanism
    • Osteryoung K.W., Pyke K.A. Plastid division: evidence for a prokaryotically derived mechanism. Curr Opin Plant Biol. 1:1998;475-479.
    • (1998) Curr Opin Plant Biol , vol.1 , pp. 475-479
    • Osteryoung, K.W.1    Pyke, K.A.2
  • 8
    • 0032516067 scopus 로고    scopus 로고
    • Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein Ftsz, an ancestral tubulin
    • A direct demonstration, by gene knockout, that FtsZ is essential for chloroplast division.
    • Strepp R., Scholz S., Kruse S., Speth V., Reski R. Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein Ftsz, an ancestral tubulin. Proc Natl Acad Sci USA. 95:1998;4368-4373. A direct demonstration, by gene knockout, that FtsZ is essential for chloroplast division.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4368-4373
    • Strepp, R.1    Scholz, S.2    Kruse, S.3    Speth, V.4    Reski, R.5
  • 9
    • 0031766756 scopus 로고    scopus 로고
    • The chloroplast division protein FtsZ is encoded by a nucleomorph gene in cryptomonads
    • Identifies an essential chloroplast protein in the reduced endosymbiont nucleus of a group of algae with second-hand plastids.
    • Fraunholz M.J., Moerschel E., Maier U.G. The chloroplast division protein FtsZ is encoded by a nucleomorph gene in cryptomonads. Mol Gen Genetics. 260:1998;207-211. Identifies an essential chloroplast protein in the reduced endosymbiont nucleus of a group of algae with second-hand plastids.
    • (1998) Mol Gen Genetics , vol.260 , pp. 207-211
    • Fraunholz, M.J.1    Moerschel, E.2    Maier, U.G.3
  • 10
    • 0032492953 scopus 로고    scopus 로고
    • Cytoskeletal proteins - The evolution of cell division
    • No direct relevance to endosymbiosis but an intriguing discussion of homology between FtsZ and tubulin and the origin of the cytoskeleton.
    • Faguy D.M., Doolittle W.F. Cytoskeletal proteins - the evolution of cell division. Curr Biol. 8:1998;338-341. No direct relevance to endosymbiosis but an intriguing discussion of homology between FtsZ and tubulin and the origin of the cytoskeleton.
    • (1998) Curr Biol , vol.8 , pp. 338-341
    • Faguy, D.M.1    Doolittle, W.F.2
  • 11
    • 0030829601 scopus 로고    scopus 로고
    • Ftsz, a tubulin homologue in prokaryote cell division
    • Erickson H.P. Ftsz, a tubulin homologue in prokaryote cell division. Trends Cell Biol. 7:1997;362-367.
    • (1997) Trends Cell Biol , vol.7 , pp. 362-367
    • Erickson, H.P.1
  • 12
    • 12644284525 scopus 로고    scopus 로고
    • Complete nucleotide sequence of the chloroplast genome from the green alga Chlorella vulgaris - The existence of genes possibly involved in chloroplast division
    • Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J., Nakashima K., Tsudzuki T., Suzuki Y.et al. Complete nucleotide sequence of the chloroplast genome from the green alga Chlorella vulgaris - the existence of genes possibly involved in chloroplast division. Proc Natl Acad Sci USA. 94:1997;5967-5972.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5967-5972
    • Wakasugi, T.1    Nagai, T.2    Kapoor, M.3    Sugita, M.4    Ito, M.5    Ito, S.6    Tsudzuki, J.7    Nakashima, K.8    Tsudzuki, T.9    Suzuki, Y.10
  • 13
    • 0033213557 scopus 로고    scopus 로고
    • Two ftsH-family genes encoded in the nuclear and chloroplast genomes of the primitive red alga Cyanidioschyzon merolae
    • in press
    • Itoh R., Takano H., Ohta N., Miyagishima S.-Y., Kuroiwa H., Kuroiwa T. Two ftsH-family genes encoded in the nuclear and chloroplast genomes of the primitive red alga Cyanidioschyzon merolae. Plant Mol Biol. 1999;. in press.
    • (1999) Plant Mol Biol
    • Itoh, R.1    Takano, H.2    Ohta, N.3    Miyagishima, S.-Y.4    Kuroiwa, H.5    Kuroiwa, T.6
  • 15
    • 0032547754 scopus 로고    scopus 로고
    • A human dynamin-related protein controls the distribution of mitochondria
    • Smirnova E., Shurland D.L., Ryazantsev S.N., Vanderbliek A.M. A human dynamin-related protein controls the distribution of mitochondria. J Cell Biol. 143:1998;351-358.
    • (1998) J Cell Biol , vol.143 , pp. 351-358
    • Smirnova, E.1    Shurland, D.L.2    Ryazantsev, S.N.3    Vanderbliek, A.M.4
  • 16
    • 0030606608 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S.et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Research. 3:1996;185-209.
    • (1996) DNA Research , vol.3 , pp. 185-209
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6    Miyajima, N.7    Hirosawa, M.8    Sugiura, M.9    Sasamoto, S.10
  • 17
    • 0032516147 scopus 로고    scopus 로고
    • Gene transfer to the nucleus and the evolution of chloroplasts
    • The first paper to make substantial use of the collected plastid genome sequences to investigate plastid evolution. Phylogenetic trees based on a massive dataset provide a strong picture of plastid history. Comparison of different gene cohorts in plastids suggests that relocation of plastid genes to the nucleus occurs frequently.
    • Martin W., Stoebe B., Goremykin V., Hansmann S., Hasegawa M., Kowallik K. Gene transfer to the nucleus and the evolution of chloroplasts. Nature. 393:1998;162-165. The first paper to make substantial use of the collected plastid genome sequences to investigate plastid evolution. Phylogenetic trees based on a massive dataset provide a strong picture of plastid history. Comparison of different gene cohorts in plastids suggests that relocation of plastid genes to the nucleus occurs frequently.
    • (1998) Nature , vol.393 , pp. 162-165
    • Martin, W.1    Stoebe, B.2    Goremykin, V.3    Hansmann, S.4    Hasegawa, M.5    Kowallik, K.6
  • 18
    • 0002160837 scopus 로고    scopus 로고
    • Gene transfer from organelles to the nucleus: How much, what happens, and why?
    • An erudite analysis of possible drivers for intracellular gene transfer. Catalogues genes transferred from endosymbiont to the host whose products are used in the host rather than being targeted back to the endosymbiont.
    • Martin W., Herrmann R.G. Gene transfer from organelles to the nucleus: how much, what happens, and why? Plant Physiol. 118:1998;9-17. An erudite analysis of possible drivers for intracellular gene transfer. Catalogues genes transferred from endosymbiont to the host whose products are used in the host rather than being targeted back to the endosymbiont.
    • (1998) Plant Physiol , vol.118 , pp. 9-17
    • Martin, W.1    Herrmann, R.G.2
  • 19
    • 7344254101 scopus 로고    scopus 로고
    • Deleterious mutation accumulation in organelle genomes
    • Lynch M., Blanchard J.L. Deleterious mutation accumulation in organelle genomes. Genetica. 103:1998;29-39.
    • (1998) Genetica , vol.103 , pp. 29-39
    • Lynch, M.1    Blanchard, J.L.2
  • 20
    • 0025850375 scopus 로고
    • Transfer of rpl22 to the nucleus greatly preceded its loss from the chloroplast and involved the gain of an intron
    • Gantt J., Baldauf S., Callie P., Weeden N., Palmer J. Transfer of rpl22 to the nucleus greatly preceded its loss from the chloroplast and involved the gain of an intron. EMBO J. 10:1991;3073-3078.
    • (1991) EMBO J , vol.10 , pp. 3073-3078
    • Gantt, J.1    Baldauf, S.2    Callie, P.3    Weeden, N.4    Palmer, J.5
  • 21
    • 0029824258 scopus 로고    scopus 로고
    • Exon shuffling and the origin of the mitochondrial targeting function in plant cytochrome c1 precursor
    • Long M., de Souza S., Rosenberg C., Gilbert W. Exon shuffling and the origin of the mitochondrial targeting function in plant cytochrome c1 precursor. Proc Natl Acad Sci USA. 93:1996;7727-7731.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7727-7731
    • Long, M.1    De Souza, S.2    Rosenberg, C.3    Gilbert, W.4
  • 22
    • 0028834427 scopus 로고
    • Transfer of rps10 from the mitochondrion to the nucleus in Arabidopsis thaliana: Evidence for RNA-mediated transfer and exon shuffling at the integration site
    • Wischmann C., Schuster W. Transfer of rps10 from the mitochondrion to the nucleus in Arabidopsis thaliana: evidence for RNA-mediated transfer and exon shuffling at the integration site. FEBS Lett. 374:1995;152-156.
    • (1995) FEBS Lett , vol.374 , pp. 152-156
    • Wischmann, C.1    Schuster, W.2
  • 23
    • 0027340233 scopus 로고
    • The presequence of cytochrome c1 from potato mitochondria is encoded on four exons
    • Wegener S., Schmitz U. The presequence of cytochrome c1 from potato mitochondria is encoded on four exons. Curr Genet. 24:1993;256-259.
    • (1993) Curr Genet , vol.24 , pp. 256-259
    • Wegener, S.1    Schmitz, U.2
  • 24
    • 0023954074 scopus 로고    scopus 로고
    • RbcS genes in Solanum tuberosum: Conservation of transit peptide and exon shuffling during evolution
    • Wolter F., Fritz C., Wilmitzer L., Schell J., Schreiber P. rbcS genes in Solanum tuberosum: conservation of transit peptide and exon shuffling during evolution. Proc Natl Acad Sci USA. 85:1998;846-850.
    • (1998) Proc Natl Acad Sci USA , vol.85 , pp. 846-850
    • Wolter, F.1    Fritz, C.2    Wilmitzer, L.3    Schell, J.4    Schreiber, P.5
  • 25
    • 0033529792 scopus 로고    scopus 로고
    • A single nuclear transcript encoding mitochondrial RPS14 and SDHB of rice is processed by alternative splicing: Common use of the same mitochondrial targeting signal for different proteins
    • Kubo N., Harada K., Hirai A., Kadowaki K.-I. A single nuclear transcript encoding mitochondrial RPS14 and SDHB of rice is processed by alternative splicing: Common use of the same mitochondrial targeting signal for different proteins. Proc Natl Acad Sci USA. 96:1999;9207-9211.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9207-9211
    • Kubo, N.1    Harada, K.2    Hirai, A.3    Kadowaki, K.-I.4
  • 26
    • 0030062188 scopus 로고    scopus 로고
    • A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare)
    • Thorbjornsen T., Villand P., Kleczkowski L., Olsen O.-A. A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare). Biochem J. 313:1996;149-154.
    • (1996) Biochem J , vol.313 , pp. 149-154
    • Thorbjornsen, T.1    Villand, P.2    Kleczkowski, L.3    Olsen, O.-A.4
  • 27
    • 0032922084 scopus 로고    scopus 로고
    • A novel plant nuclear gene encoding chloroplast ribosomal protein S9 has a transit peptide related to that of rice chloroplast ribosomal protein L12
    • Arimura S., Takusagawa S., Hatano S., Nakazono M., Hirai A., Tsutsumi N. A novel plant nuclear gene encoding chloroplast ribosomal protein S9 has a transit peptide related to that of rice chloroplast ribosomal protein L12. FEBS Letts. 450:1999;231-234.
    • (1999) FEBS Letts , vol.450 , pp. 231-234
    • Arimura, S.1    Takusagawa, S.2    Hatano, S.3    Nakazono, M.4    Hirai, A.5    Tsutsumi, N.6
  • 28
    • 0033582158 scopus 로고    scopus 로고
    • The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: Identification of a cyanobacterial homolog
    • A key experimental analysis of Toc75 homologues in Synechocystis, a cyanobacterium related to the ancestor of chloroplasts. The authors develop fascinating hypotheses to explain how a channel that initially secreted proteins across the outer, Gram-negative, cyanobacterial membrane could be turned inside-out via gene transfer in endosymbiosis and caused to run backwards by using the secretion substrate as leader peptides on cytoplasmically synthesised gene products.
    • Reumann S., Davila-Aponte J., Keegstra K. The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc Natl Acad Sci USA. 96:1999;784-789. A key experimental analysis of Toc75 homologues in Synechocystis, a cyanobacterium related to the ancestor of chloroplasts. The authors develop fascinating hypotheses to explain how a channel that initially secreted proteins across the outer, Gram-negative, cyanobacterial membrane could be turned inside-out via gene transfer in endosymbiosis and caused to run backwards by using the secretion substrate as leader peptides on cytoplasmically synthesised gene products.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 784-789
    • Reumann, S.1    Davila-Aponte, J.2    Keegstra, K.3
  • 29
    • 0344734090 scopus 로고    scopus 로고
    • GFP for in vivo imaging of subcellular structures in plant cells
    • This article includes links to web movies of green fluorescent protein targeted to plant organelles including the extraordinary tubules interconnecting chloroplasts.
    • Kohler R. GFP for in vivo imaging of subcellular structures in plant cells. Trends Plant Sci. 3:1998;317-320. This article includes links to web movies of green fluorescent protein targeted to plant organelles including the extraordinary tubules interconnecting chloroplasts.
    • (1998) Trends Plant Sci , vol.3 , pp. 317-320
    • Kohler, R.1
  • 30
    • 0032252226 scopus 로고    scopus 로고
    • Screening of cDNA clones for plastid-targeted proteins
    • Shimada Y., Wu G.-J., Watanabe A. Screening of cDNA clones for plastid-targeted proteins. Plant Mol Biol Rep. 16:1998;199-200.
    • (1998) Plant Mol Biol Rep , vol.16 , pp. 199-200
    • Shimada, Y.1    Wu, G.-J.2    Watanabe, A.3
  • 31
    • 0032784582 scopus 로고    scopus 로고
    • The structural flexibility of the preferredoxin transit peptide
    • The first paper to define a secondary structure for transit peptides in relation to the target membrane.
    • Wienk H.L.J., Czisch M., de Kruijff B. The structural flexibility of the preferredoxin transit peptide. FEBS Lett. 453:1999;318-326. The first paper to define a secondary structure for transit peptides in relation to the target membrane.
    • (1999) FEBS Lett , vol.453 , pp. 318-326
    • Wienk, H.L.J.1    Czisch, M.2    De Kruijff, B.3
  • 32
    • 0032169930 scopus 로고    scopus 로고
    • The role of lipids in plastid protein transport
    • A comprehensive review of models for galactolipid and transit peptide interactions.
    • Bruce B.D. The role of lipids in plastid protein transport. Plant Mol Biol. 38:1998;223-246. A comprehensive review of models for galactolipid and transit peptide interactions.
    • (1998) Plant Mol Biol , vol.38 , pp. 223-246
    • Bruce, B.D.1
  • 33
    • 0007549942 scopus 로고
    • A new hypothesis for the mechanism of protein translocation into chloroplasts
    • W. Briggs. New York: Alan R Liss
    • Keegstra K. A new hypothesis for the mechanism of protein translocation into chloroplasts. Briggs W. Photosynthesis. 1989;347-357 Alan R Liss, New York.
    • (1989) Photosynthesis , pp. 347-357
    • Keegstra, K.1
  • 34
    • 0032189210 scopus 로고    scopus 로고
    • Mutant deficient in the plastid lipid dgd is defective in protein import into chloroplasts
    • Chen L.J., Li H.M.A. mutant deficient in the plastid lipid dgd is defective in protein import into chloroplasts. Plant J. 16:1998;33-39.
    • (1998) Plant J , vol.16 , pp. 33-39
    • Chen, L.J.1    Li, H.M.A.2
  • 35
    • 0030901255 scopus 로고    scopus 로고
    • Galactolipid biosynthesis genes and endosymbiosis
    • Slabas T. Galactolipid biosynthesis genes and endosymbiosis. Trends Plant Sci. 2:1997;161-162.
    • (1997) Trends Plant Sci , vol.2 , pp. 161-162
    • Slabas, T.1
  • 37
    • 0242504168 scopus 로고    scopus 로고
    • Arabidopsis galactolipid biosynthesis and lipid trafficking mediated by DGD1
    • Dormann P., Balbo I., Benning C. Arabidopsis galactolipid biosynthesis and lipid trafficking mediated by DGD1. Science. 284:1999;2181-2184.
    • (1999) Science , vol.284 , pp. 2181-2184
    • Dormann, P.1    Balbo, I.2    Benning, C.3
  • 38
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • From the people who brought you SignalP for identification of signal peptides. This paper describes an informatics tool for identification of chloroplast transit peptides in plants. See URL
    • Emanuelsson O., Nielsen H., von Heijne G. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8:1999;978-984. From the people who brought you SignalP for identification of signal peptides. This paper describes an informatics tool for identification of chloroplast transit peptides in plants. See URL http://www.cbs.dtu.dk/services/ChloroP/.
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 39
    • 0027961026 scopus 로고
    • SecA homolog in protein transport within chloroplasts: Evidence for endosymbiont-derived sorting
    • Yuan J., Henry R., McCaffrey M., Cline K.J. SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting. Science. 266:1994;796-798.
    • (1994) Science , vol.266 , pp. 796-798
    • Yuan, J.1    Henry, R.2    McCaffrey, M.3    Cline, K.J.4
  • 40
    • 0032550223 scopus 로고    scopus 로고
    • A secY homologue is required for the elaboration of the chloroplast thylakoid membrane and for normal chloroplast gene expression
    • Roy L.M., Barkan A. A secY homologue is required for the elaboration of the chloroplast thylakoid membrane and for normal chloroplast gene expression. J Cell Biol. 141:1998;385-395.
    • (1998) J Cell Biol , vol.141 , pp. 385-395
    • Roy, L.M.1    Barkan, A.2
  • 41
    • 0033534784 scopus 로고    scopus 로고
    • Functional divergence of the plastid and cytosolic forms of the 54-kDa subunit of signal recognition particle
    • Schuenemann D., Amin P., Hoffman N.E. Functional divergence of the plastid and cytosolic forms of the 54-kDa subunit of signal recognition particle. Biochem Biophys Res Comm. 254:1999;253-258.
    • (1999) Biochem Biophys Res Comm , vol.254 , pp. 253-258
    • Schuenemann, D.1    Amin, P.2    Hoffman, N.E.3
  • 42
    • 0033597136 scopus 로고    scopus 로고
    • Chloroplast SecY is complexed to SecE and involved in the translocation of the 33-kDa but not the 23-kDa subunit of the oxygen-evolving complex
    • Schuenemann D., Amin P., Hartmann E., Hoffman N.E. Chloroplast SecY is complexed to SecE and involved in the translocation of the 33-kDa but not the 23-kDa subunit of the oxygen-evolving complex. J Biol Chem. 274:1999;12177-12182.
    • (1999) J Biol Chem , vol.274 , pp. 12177-12182
    • Schuenemann, D.1    Amin, P.2    Hartmann, E.3    Hoffman, N.E.4
  • 44
    • 0031975202 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana - implications for the origin and catalytic mechanism of the enzyme
    • Chaal B.K., Mould R.M., Barbrook A.C., Gray J.C., Howe C.J. Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana - implications for the origin and catalytic mechanism of the enzyme. J Biol Chem. 273:1998;689-692.
    • (1998) J Biol Chem , vol.273 , pp. 689-692
    • Chaal, B.K.1    Mould, R.M.2    Barbrook, A.C.3    Gray, J.C.4    Howe, C.J.5
  • 45
    • 0031736218 scopus 로고    scopus 로고
    • Old and new pathways of protein export in chloroplasts and bacteria
    • Settles A.M., Martienssen R. Old and new pathways of protein export in chloroplasts and bacteria. Trends Cell Biol. 8:1998;494-501.
    • (1998) Trends Cell Biol , vol.8 , pp. 494-501
    • Settles, A.M.1    Martienssen, R.2
  • 46
    • 0032168004 scopus 로고    scopus 로고
    • Protein translocation into and across the chloroplastic envelope membranes
    • Soll J., Tien R. Protein translocation into and across the chloroplastic envelope membranes. Plant Mol Biol. 38:1998;191-207.
    • (1998) Plant Mol Biol , vol.38 , pp. 191-207
    • Soll, J.1    Tien, R.2
  • 47
    • 0032004983 scopus 로고    scopus 로고
    • The protein translocation apparatus of chloroplast envelopes
    • Heins L., Collinson I., Soll J. The protein translocation apparatus of chloroplast envelopes. Trends Plant Sci. 3:1998;56-61.
    • (1998) Trends Plant Sci , vol.3 , pp. 56-61
    • Heins, L.1    Collinson, I.2    Soll, J.3
  • 48
    • 0031397350 scopus 로고    scopus 로고
    • Mechanism of protein transport across the chloroplast envelope
    • Fuks B., Schnell D.J. Mechanism of protein transport across the chloroplast envelope. Plant Physiol. 114:1997;405-410.
    • (1997) Plant Physiol , vol.114 , pp. 405-410
    • Fuks, B.1    Schnell, D.J.2
  • 49
    • 0033179289 scopus 로고    scopus 로고
    • The endosymbiotic origin of the protein import machinery of chloroplastid envelope membranes
    • A detailed database analysis of possible homologues of chloroplast transport machinery in cyanobacteria the ancestors of the chloroplast endosymbiont.
    • Reumann S., Keegstra K. The endosymbiotic origin of the protein import machinery of chloroplastid envelope membranes. Trends Plant Sci. 4:1999;302-307. A detailed database analysis of possible homologues of chloroplast transport machinery in cyanobacteria the ancestors of the chloroplast endosymbiont.
    • (1999) Trends Plant Sci , vol.4 , pp. 302-307
    • Reumann, S.1    Keegstra, K.2
  • 50
    • 0033030860 scopus 로고    scopus 로고
    • Chloroplast precursor protein translocon
    • May T., Soll J. Chloroplast precursor protein translocon. FEBS Letts. 452:1999;52-56.
    • (1999) FEBS Letts , vol.452 , pp. 52-56
    • May, T.1    Soll, J.2
  • 51
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • A detailed review of the protein import system of chloroplasts with a strong focus on internal sorting.
    • Keegstra K., Cline K. Protein import and routing systems of chloroplasts. Plant Cell. 11:1999;557-570. A detailed review of the protein import system of chloroplasts with a strong focus on internal sorting.
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 52
    • 0032419712 scopus 로고    scopus 로고
    • Origin of a chloroplast protein importer
    • A key paper that identifies a homologue of a central chloroplast protein import component (Toc75) in the cyanobacterium Synechocystis. The Synechocystis version is shown to have an identical structure and to be located in the equivalent membrane providing a strong proof of endosymbiosis as well as confirmation that the outer membrane of chloroplasts derives from the outer membrane of Gram-negative cyanobacteria.
    • Bölter B., Soll J., Schulz A., Hinnah S., Wagner R. Origin of a chloroplast protein importer. Proc Natl Acad Sci USA. 95:1998;15831-15836. A key paper that identifies a homologue of a central chloroplast protein import component (Toc75) in the cyanobacterium Synechocystis. The Synechocystis version is shown to have an identical structure and to be located in the equivalent membrane providing a strong proof of endosymbiosis as well as confirmation that the outer membrane of chloroplasts derives from the outer membrane of Gram-negative cyanobacteria.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15831-15836
    • Bölter, B.1    Soll, J.2    Schulz, A.3    Hinnah, S.4    Wagner, R.5
  • 53
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • Hinnah S.C., Hill K., Wagner R., Schlicher T., Soll J. Reconstitution of a chloroplast protein import channel. EMBO J. 16:1997;7351-7360.
    • (1997) EMBO J , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 54
    • 0032563173 scopus 로고    scopus 로고
    • Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels
    • Hypothesis paper suggesting that beta-barrel membrane channels are a broad family of proteins with roles in membrane transport in bacteria.
    • Bainbridge G., Gokce I., Lakey J.H. Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels. FEBS Letts. 431:1998;305-308. Hypothesis paper suggesting that beta-barrel membrane channels are a broad family of proteins with roles in membrane transport in bacteria.
    • (1998) FEBS Letts , vol.431 , pp. 305-308
    • Bainbridge, G.1    Gokce, I.2    Lakey, J.H.3
  • 55
    • 0032510319 scopus 로고    scopus 로고
    • Chloroplast biogenesis - mixing the prokaryotic and the eukaryotic
    • Heins L., Soll J. Chloroplast biogenesis - mixing the prokaryotic and the eukaryotic. Curr Biol. 8:1998;215-217.
    • (1998) Curr Biol , vol.8 , pp. 215-217
    • Heins, L.1    Soll, J.2
  • 56
    • 0030293036 scopus 로고    scopus 로고
    • Novel, bipartite transit peptide targets OEP75 to the outer membrane of the chloroplastic envelope
    • Tranel P.J., Keegstra K.A. novel, bipartite transit peptide targets OEP75 to the outer membrane of the chloroplastic envelope. Plant Cell. 8:1996;2093-2104.
    • (1996) Plant Cell , vol.8 , pp. 2093-2104
    • Tranel, P.J.1    Keegstra, K.A.2
  • 57
    • 0032553430 scopus 로고    scopus 로고
    • The isolated complex of the translocase of the outer membrane of mitochondria - characterization of the cation-selective and voltage-gated preprotein-conducting pore
    • Kunkele K.P., Juin P., Pompa C., Nargang F.E., Henry J.P., Neupert W., Lill R., Thieffry M. The isolated complex of the translocase of the outer membrane of mitochondria - characterization of the cation-selective and voltage-gated preprotein-conducting pore. J Biol Chem. 273:1998;31032-31039.
    • (1998) J Biol Chem , vol.273 , pp. 31032-31039
    • Kunkele, K.P.1    Juin, P.2    Pompa, C.3    Nargang, F.E.4    Henry, J.P.5    Neupert, W.6    Lill, R.7    Thieffry, M.8
  • 58
    • 0033548261 scopus 로고    scopus 로고
    • The preprotein translocase of the mitochondrial inner membrane: Function and evolution
    • Rassow J., Dekker P.J.T., van Wilpe S., Meijer M., Soll J. The preprotein translocase of the mitochondrial inner membrane: function and evolution. J Mol Biol. 286:1999;105-120.
    • (1999) J Mol Biol , vol.286 , pp. 105-120
    • Rassow, J.1    Dekker, P.J.T.2    Van Wilpe, S.3    Meijer, M.4    Soll, J.5
  • 59
  • 60
    • 0033167259 scopus 로고    scopus 로고
    • Plastids and protein targeting
    • Yet another sesquipedalian offering from the McFadden review factory. Explores intracellular gene transfer with emphasis on secondary endosymbiosis and nucleomorphs.
    • McFadden G.I. Plastids and protein targeting. J Euk Microbiol. 46:1999;339-346. Yet another sesquipedalian offering from the McFadden review factory. Explores intracellular gene transfer with emphasis on secondary endosymbiosis and nucleomorphs.
    • (1999) J Euk Microbiol , vol.46 , pp. 339-346
    • McFadden, G.I.1
  • 61
    • 0344549379 scopus 로고    scopus 로고
    • Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum
    • The first paper to identify nuclear-encoded proteins targeted to the relict chloroplast of the malaria parasite. Green fluorescent protein targeting is used to demonstrate that the leader is sufficient for targeting across the four plastid bounding membranes. This work provides the first clues about a possible function of relict plastid in fatty acid biosynthesis.
    • Waller R.F., Keeling P.J., Donald R.G.K., Striepen B., Handman E., Lang, Unnasch N., Cowman A.F., Besra G.S., Roos D.S., McFadden G.I. Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum. Proc Natl Acad Sci USA. 95:1998;12352-12357. The first paper to identify nuclear-encoded proteins targeted to the relict chloroplast of the malaria parasite. Green fluorescent protein targeting is used to demonstrate that the leader is sufficient for targeting across the four plastid bounding membranes. This work provides the first clues about a possible function of relict plastid in fatty acid biosynthesis.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12352-12357
    • Waller, R.F.1    Keeling, P.J.2    Donald, R.G.K.3    Striepen, B.4    Handman, E.5    Lang6    Unnasch, N.7    Cowman, A.F.8    Besra, G.S.9    Roos, D.S.10    McFadden, G.I.11
  • 62
    • 0032553297 scopus 로고    scopus 로고
    • Protein transport into complex diatom plastids utilizes two different targeting signals
    • Analyses of leader function for nuclear-encoded plastid proteins of diatoms. Demonstrates that diatom transit peptides mediate uptake by plant chloroplasts thereby suggesting that the systems are partially conserved.
    • Lang M., Apt K.E., Kroth P.G. Protein transport into complex diatom plastids utilizes two different targeting signals. J Biol Chem. 273:1998;30973-30978. Analyses of leader function for nuclear-encoded plastid proteins of diatoms. Demonstrates that diatom transit peptides mediate uptake by plant chloroplasts thereby suggesting that the systems are partially conserved.
    • (1998) J Biol Chem , vol.273 , pp. 30973-30978
    • Lang, M.1    Apt, K.E.2    Kroth, P.G.3
  • 63
    • 0032955849 scopus 로고    scopus 로고
    • Topology of Euglena chloroplast protein precursors within the endoplasmic reticulum to Golgi to chloroplast transport vesicles
    • Sulli C., Fang Z.W., Muchal U., Schwartzbach S.D. Topology of Euglena chloroplast protein precursors within the endoplasmic reticulum to Golgi to chloroplast transport vesicles. J Biol Chem. 274:1999;457-463.
    • (1999) J Biol Chem , vol.274 , pp. 457-463
    • Sulli, C.1    Fang, Z.W.2    Muchal, U.3    Schwartzbach, S.D.4
  • 64
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G., Dobberstein B. Common principles of protein translocation across membranes. Science. 271:1996;1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 65
    • 0018331207 scopus 로고
    • The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER
    • Gibbs S.P. The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER. J Cell Sci. 35:1979;253-266.
    • (1979) J Cell Sci , vol.35 , pp. 253-266
    • Gibbs, S.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.