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Analysis of ftsZ function using transgenics in Arabidopsis. The first identification of ftsZ genes whose products may function in the eukaryotic cytoplasm.
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Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein Ftsz, an ancestral tubulin
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A direct demonstration, by gene knockout, that FtsZ is essential for chloroplast division.
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Strepp, R.1
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The chloroplast division protein FtsZ is encoded by a nucleomorph gene in cryptomonads
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Identifies an essential chloroplast protein in the reduced endosymbiont nucleus of a group of algae with second-hand plastids.
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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.
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Cytoskeletal proteins - The evolution of cell division
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No direct relevance to endosymbiosis but an intriguing discussion of homology between FtsZ and tubulin and the origin of the cytoskeleton.
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Two ftsH-family genes encoded in the nuclear and chloroplast genomes of the primitive red alga Cyanidioschyzon merolae
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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
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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.
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The protein translocation apparatus of chloroplast envelopes
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Heins L., Collinson I., Soll J. The protein translocation apparatus of chloroplast envelopes. Trends Plant Sci. 3:1998;56-61.
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Heins, L.1
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Mechanism of protein transport across the chloroplast envelope
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Fuks B., Schnell D.J. Mechanism of protein transport across the chloroplast envelope. Plant Physiol. 114:1997;405-410.
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49
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The endosymbiotic origin of the protein import machinery of chloroplastid envelope membranes
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A detailed database analysis of possible homologues of chloroplast transport machinery in cyanobacteria the ancestors of the chloroplast endosymbiont.
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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.
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Trends Plant Sci
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Reumann, S.1
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50
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Chloroplast precursor protein translocon
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May T., Soll J. Chloroplast precursor protein translocon. FEBS Letts. 452:1999;52-56.
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FEBS Letts
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May, T.1
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Protein import and routing systems of chloroplasts
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A detailed review of the protein import system of chloroplasts with a strong focus on internal sorting.
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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.
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Keegstra, K.1
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52
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Origin of a chloroplast protein importer
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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.
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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.
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Proc Natl Acad Sci USA
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Soll, J.2
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Wagner, R.5
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53
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Reconstitution of a chloroplast protein import channel
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Hinnah S.C., Hill K., Wagner R., Schlicher T., Soll J. Reconstitution of a chloroplast protein import channel. EMBO J. 16:1997;7351-7360.
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Soll, J.5
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54
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Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels
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Hypothesis paper suggesting that beta-barrel membrane channels are a broad family of proteins with roles in membrane transport in bacteria.
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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.
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FEBS Letts
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Bainbridge, G.1
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55
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Chloroplast biogenesis - mixing the prokaryotic and the eukaryotic
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Heins L., Soll J. Chloroplast biogenesis - mixing the prokaryotic and the eukaryotic. Curr Biol. 8:1998;215-217.
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(1998)
Curr Biol
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Heins, L.1
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56
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Novel, bipartite transit peptide targets OEP75 to the outer membrane of the chloroplastic envelope
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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.
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Tranel, P.J.1
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57
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0032553430
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The isolated complex of the translocase of the outer membrane of mitochondria - characterization of the cation-selective and voltage-gated preprotein-conducting pore
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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.
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Kunkele, K.P.1
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Thieffry, M.8
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58
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The preprotein translocase of the mitochondrial inner membrane: Function and evolution
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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.
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J Mol Biol
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Rassow, J.1
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60
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Plastids and protein targeting
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Yet another sesquipedalian offering from the McFadden review factory. Explores intracellular gene transfer with emphasis on secondary endosymbiosis and nucleomorphs.
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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.
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J Euk Microbiol
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McFadden, G.I.1
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Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum
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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.
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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.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 12352-12357
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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
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62
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Protein transport into complex diatom plastids utilizes two different targeting signals
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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.
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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.
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(1998)
J Biol Chem
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Lang, M.1
Apt, K.E.2
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Topology of Euglena chloroplast protein precursors within the endoplasmic reticulum to Golgi to chloroplast transport vesicles
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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.
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J Biol Chem
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Sulli, C.1
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Schatz G., Dobberstein B. Common principles of protein translocation across membranes. Science. 271:1996;1519-1526.
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Science
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The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER
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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.
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