ArticleThe Journal of cell biology1990
The chloroplast import receptor is an integral membrane protein of chloroplast envelope contact sites.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 100 citations in OpenAlex.
- Lipid transport required to make lipids of photosynthetic membranes.Photosynthesis research · 2018Review
- Differential transit peptide recognition during preprotein binding and translocation into flowering plant plastids.The Plant cell · 2012Article
- Deletion of the chloroplast-localized Thylakoid formation1 gene product in Arabidopsis leads to deficient thylakoid formation and variegated leaves.Plant physiology · 2004Article
- Prediction of the plant beta-barrel proteome: a case study of the chloroplast outer envelope.Protein science : a publication of the Protein Society · 2003Article
- Maize non-photosynthetic ferredoxin precursor is mis-sorted to the intermembrane space of chloroplasts in the presence of light.Plant physiology · 2001Article
- A mammalian cytochrome fused to a chloroplast transit peptide is a functional haemoprotein and is imported into isolated chloroplasts.The Biochemical journal · 2000Article
- Tic20 and Tic22 are new components of the protein import apparatus at the chloroplast inner envelope membrane.The Journal of cell biology · 1998Article
- Interaction of the protein import and folding machineries of the chloroplast.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implications.The Journal of cell biology · 1996Article
- Assembly of the chlorophyll-protein complexes.Photosynthesis research · 1995Article
- Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes.Plant molecular biology · 1994Article
- Substrate- and species-specific processing enzymes for chloroplast precursor proteins.The Biochemical journal · 1994Article
- Expression of genes encoding the tobacco chloroplast phosphate translocator is not light-regulated and is repressed by sucrose.Molecular & general genetics : MGG · 1994Article
- Envelope membrane proteins that interact with chloroplastic precursor proteins.The Plant cell · 1994Article
- Article
- Antisense repression of the chloroplast triose phosphate translocator affects carbon partitioning in transgenic potato plants.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Expression of the triose phosphate translocator gene from potato is light dependent and restricted to green tissues.Molecular & general genetics : MGG · 1993Article
- Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metal-affinity chromatography step.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Identification of intermediates in the pathway of protein import into chloroplasts and their localization to envelope contact sites.The Journal of cell biology · 1993Article
- Import of proteins into peroxisomes and other microbodies.The Biochemical journal · 1992Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A chloroplast import receptor from pea, previously identified by antiidiotypic antibodies was purified and its primary structure deduced from its cDNA sequence. The protein is a 36-kD integral membrane protein (p36) with eight potential transmembrane segments. Fab prepared from monospecific anti-p36 IgG inhibits the import of the ribulose-1,5-bisphosphate carboxylase small subunit precursor (pS) by interfering with pS binding at the chloroplast surface. Anti-p36 IgGs are able to immunoprecipitate a Triton X-100 soluble p36-pS complex, suggesting a direct interaction between p36 and pS. This immunoprecipitation was specific as it was abolished by a pS synthetic transit peptide, consistent with the transit sequence receptor function of p36. Immunoelectron microscopy localized p36 to regions of the outer chloroplast membrane that are in close contact with the inner chloroplast membrane. Comparison of the deduced sequence of pea p36 to that of other known proteins indicates a striking homology to a protein from spinach chloroplasts that was previously suggested to be the triose phosphate-3-phosphoglycerate-phosphate translocator (phosphate translocator) (Flügge, U. I., K. Fischer, A. Gross, W. Sebald, F. Lottspeich, and C. Eckerskorn. 1989. EMBO (Eur. Mol. Biol. Organ.) J. 8:39-46). However, incubation of Triton X-100 solubilized chloroplast envelope material with hydroxylapatite indicated that p36 was quantitatively absorbed, whereas previous reports have shown that phosphate translocator activity does not bind to hydroxylapatite (Flügge, U. I., and H. W. Heldt. 1981. Biochim. Biophys. Acta. 638:296-304. These data, in addition to the topology and import inhibition data presented in this report support the assignment of p36 as a receptor for chloroplast protein import, and argue against the assignment of the spinach homologue of this protein as the chloroplast phosphate translocator.
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