ArticleThe Plant cell1996
A novel, bipartite transit peptide targets OEP75 to the outer membrane of the chloroplastic envelope.
Article in The Plant cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- New Insights into the Chloroplast Outer Membrane Proteome and Associated Targeting Pathways.International journal of molecular sciences · 2022Review
- Molecular characterization, targeting and expression analysis of chloroplast and mitochondrion protein import components inFrontiers in plant science · 2022Article
- Insertion of plastidic β-barrel proteins into the outer envelopes of plastids involves an intermembrane space intermediate formed with Toc75-V/OEP80.The Plant cell · 2021Article
- Go your own way: membrane-targeting sequences.Plant physiology · 2021Article
- Toc75-V/OEP80 is processed during translocation into chloroplasts, and the membrane-embedded form exposes its POTRA domain to the intermembrane space.FEBS open bio · 2020Article
- Chloroplast Outer Membrane β-Barrel Proteins Use Components of the General Import Apparatus.The Plant cell · 2019Article
- Biogenesis of chloroplast outer envelope membrane proteins.Plant cell reports · 2019Review
- Evolution of protein transport to the chloroplast envelope membranes.Photosynthesis research · 2018Review
- Polypeptide Transport-Associated Domains of the Toc75 Channel Protein Are Located in the Intermembrane Space of Chloroplasts.Plant physiology · 2016Article
- Article
- Polyglycine Acts as a Rejection Signal for Protein Transport at the Chloroplast Envelope.PloS one · 2016Article
- New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Journal of molecular biology · 2015Review
- Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane.Frontiers in plant science · 2014Review
- Evolution and targeting of Omp85 homologs in the chloroplast outer envelope membrane.Frontiers in plant science · 2014Article
- The selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes.Frontiers in plant science · 2014Article
- Specific targeting of proteins to outer envelope membranes of endosymbiotic organelles, chloroplasts, and mitochondria.Frontiers in plant science · 2014Review
- Chloroplast β-barrel proteins are assembled into the mitochondrial outer membrane in a process that depends on the TOM and TOB complexes.The Journal of biological chemistry · 2012Article
- A transit peptide-like sorting signal at the C terminus directs the Bienertia sinuspersici preprotein receptor Toc159 to the chloroplast outer membrane.The Plant cell · 2012Article
- OEP80, an essential protein paralogous to the chloroplast protein translocation channel Toc75, exists as a 70-kD protein in the Arabidopsis thaliana chloroplast outer envelope.Plant molecular biology · 2012Article
- Chloroplast Omp85 proteins change orientation during evolution.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
OEP75 is an outer envelope membrane component of the chloroplastic protein import apparatus and is synthesized in the cytoplasm as a higher molecular weight precursor (prOEP75). During its own import, prOEP75 is processed first to an intermediate (iOEP75) and subsequently to the mature form (mOEP75). Experiments conducted with stromal extracts indicated that iOEP75 was generated from prOEP75 by the activity of the stromal processing peptidase. The specific processing site was determined and used to divide the prOEP75 transit peptide into N- and C-terminal domains. To determine the targeting functions of the two domains of the transit peptide and of the mature region of prOEP75, we created a deletion mutant construct from prOEP75 and chimeric constructs between domains of prOEP75 and the precursor to a small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. Analysis of these constructs by in vitro chloroplastic protein import assays revealed that the transit peptide of prOEP75 is bipartite in that the N- and C-terminal portions contain chloroplastic and intraorganellar targeting information, respectively.
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