Stage-dependent localization of LHCP II apoprotein in the Golgi of synchronized cells of Euglena gracilis by immunogold electron microscopy

Osafune, Tetsuaki; Schiff, Jerome A.; Hase, Eiji

doi:10.1016/0014-4827(91)90103-2

Cited by 46 publications

(25 citation statements)

References 10 publications

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“…Immunoelectron microscopy (37,38) and pulse-chase intracellular localization studies (13,14) have clearly demonstrated that protein import into Euglena chloroplasts is fundamentally different from import into chloroplasts with a double envelope membrane. Euglena precursors are co-translationally inserted into the ER, transported as integral membrane proteins from the ER to the Golgi apparatus and from the Golgi apparatus to the outermost of the three Euglena envelope membranes, and then imported through the middle and inner chloroplast envelope membranes (13-14, 37, 38).…”

Section: Discussionmentioning

confidence: 99%

Topology of Euglena Chloroplast Protein Precursors within Endoplasmic Reticulum to Golgi to Chloroplast Transport Vesicles

Sulli

Fang

Muchhal³

et al. 1999

Journal of Biological Chemistry

134

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Section: Discussionmentioning

confidence: 99%

Topology of Euglena Chloroplast Protein Precursors within Endoplasmic Reticulum to Golgi to Chloroplast Transport Vesicles

Sulli

Fang

Muchhal³

et al. 1999

Journal of Biological Chemistry

134

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“…Yet it has not been possible to reliably detect PTS intermediates associated with secretory structures such as the ER-Golgi membranes. Pulse-chase and immunoelectronmicroscopy studies in Euglena, suggest that there is transport from the Golgi to the plastid (8,13). In P. falciparum, a detailed electron microscopy study shows membrane-bound ribosomes in close apposition to the plastid (14), suggesting that there may be direct membrane connections between the ER and the plastid.…”

mentioning

confidence: 99%

Targeting the Malarial Plastid via the Parasitophorous Vacuole

Cheresh

Harrison

Fujioka

et al. 2002

Journal of Biological Chemistry

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The malarial "apicoplast" derived from an algal plastid, has stimulated interest for its novel evolutionary biology and potential as a drug target. An endoplasmic reticulum-type signal sequence followed by a plastid targeting sequence are required to target proteins to the apicoplast but the pathway by which proteins are transported to the organelle is unknown. By stage regulating the expression of transgenes we show that early (0 -12 h) in the parasite's development in red cells, newly synthesized green fluorescent protein that contains the plastid targeting sequence (plastid targeting sequence-green fluorescent protein (PTS-GFP)) is recruited into the parasite's secretory pathway. PTS-GFP in 0 -12-h parasites is found released into the parasitophorous vacuole (PV) and in apposition with the Golgi. However, import into the apicoplast and processing to GFP does not occur until 18 -36 h in development. In intermediate, 18-h parasites PTS-GFP resides in the PV. Quantitative exit of PTS-GFP from the PV and its conversion to GFP is seen at 36 h. The data suggest that: (i) import into the apicoplast is stage regulated and (ii) the PTS can signal endomembrane targeting from the PV to the apicoplast.

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“…Euglena pLHCPII is synthesized on membrane-bound ribosomes as found for proteins transported into the endoplasmic reticulum (ER) rather than on free ribosomes as normally found for cytoplasmically synthesized chloroplast proteins (4,11). Immunogold electron microscopy localizes Euglena LHCPII to the Golgi apparatus and chloroplast when LHCPII is being synthesized, while at times when LHCPII is not being synthesized, an immunoreaction is seen only in the chloroplast (10,13). It thus appears that Euglena pLHCPII is transported into the ER prior to chloroplast localization.…”

mentioning

confidence: 99%

The presequence of Euglena LHCPII, a cytoplasmically synthesized chloroplast protein, contains a functional endoplasmic reticulum-targeting domain.

Kishore

Muchhal

Schwartzbach

1993

Proc. Natl. Acad. Sci. U.S.A.

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The precursor to the Euglena light-harvesting chlorophyll a/b-binding protein of photosystem II (pLHCPII) is unique; it is a polyprotein, synthesized on membrane-bound ribosomes and transported to the Golgi apparatus prior to chloroplast localization. A cDNA corresponding to the 5' end of LHCPII mRNA has been isolated and sequenced. The deduced amino acid sequence of this cDNA indicates that Euglena pLHCPII contains a 141-amino acid N-terminal extension. The N-terminal extension contains three hydrophobic domains and a potential signal peptidase cleavage site at amino acid 35. Cotranslational processing by canine microsomes removed approximately 35 amino acids from an in vitro synthesized 33-kDa pLHCPII composed of a 141-amino acid N-terminal extension and a 180-amino acid partial LH-CPU unit truncated at the beginning of the third membranespanning hydrophobic domain. Processed pLHCPII was degraded by exogenous protease, indicating that it had not been translocated to the microsomal lumen. Extraction with 0.1 M Na2CO3, pH 11.5, did not remove the processed pLHCPII from the microsomal membrane. A stop-transfer membrane anchor sequence appears to anchor the nascent protein within the membrane, preventing translocation into the lumen. Taken together, these results provide biochemical evidence for a functional cleaved signal sequence within the N-terminal extension of a Euglena cytoplasmically synthesized chloroplastlocalized protein.

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Stage-dependent localization of LHCP II apoprotein in the Golgi of synchronized cells of Euglena gracilis by immunogold electron microscopy

Cited by 46 publications

References 10 publications

Topology of Euglena Chloroplast Protein Precursors within Endoplasmic Reticulum to Golgi to Chloroplast Transport Vesicles

Topology of Euglena Chloroplast Protein Precursors within Endoplasmic Reticulum to Golgi to Chloroplast Transport Vesicles

Targeting the Malarial Plastid via the Parasitophorous Vacuole

The presequence of Euglena LHCPII, a cytoplasmically synthesized chloroplast protein, contains a functional endoplasmic reticulum-targeting domain.

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