ArticlePlant physiology2008
The Omp85-related chloroplast outer envelope protein OEP80 is essential for viability in Arabidopsis.
Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 80 citations in OpenAlex.
- Biochemical characterisation supports a central role for Oep80 from Arabidopsis thaliana in chloroplastic β-barrel protein assembly.Communications biology · 2025Article
- Probing the physiological role of the plastid outer-envelope membrane using the oemiR plasmid collection.G3 (Bethesda, Md.) · 2023Article
- Article
- Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Article
- New Insights into the Chloroplast Outer Membrane Proteome and Associated Targeting Pathways.International journal of molecular sciences · 2022Review
- 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
- BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.Molecular cell · 2021Article
- Article
- 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
- Barreling Down the Chloroplast Highway: Protein Sorting of Outer-Membrane β-Barrel Proteins.The Plant cell · 2019Article
- Biogenesis of chloroplast outer envelope membrane proteins.Plant cell reports · 2019Review
- Proteomic Analysis of ArabidopsisFrontiers in plant science · 2019Article
- Evolution of protein transport to the chloroplast envelope membranes.Photosynthesis research · 2018Review
- The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Fitting the Pieces of the β-Barrel Assembly Machinery Complex.Biochemistry · 2015Review
- The Omp85-type outer membrane protein p36 of Arabidopsis thaliana evolved by recent gene duplication.Journal of plant research · 2015Article
- Inhibition of the β-barrel assembly machine by a peptide that binds BamD.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Natural variation in sensitivity to a loss of chloroplast translation in Arabidopsis.Plant physiology · 2014Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
beta-Barrel proteins of the Omp85 (Outer membrane protein, 85 kD) superfamily exist in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. Prominent Omp85 proteins in bacteria and mitochondria mediate biogenesis of other beta-barrel proteins and are indispensable for viability. In Arabidopsis (Arabidopsis thaliana) chloroplasts, there are two distinct types of Omp85-related protein: Toc75 (Translocon at the outer envelope membrane of chloroplasts, 75 kD) and OEP80 (Outer Envelope Protein, 80 kD). Toc75 functions as a preprotein translocation channel during chloroplast import, but the role of OEP80 remains elusive. We characterized three T-DNA mutants of the Arabidopsis OEP80 (AtOEP80) gene. Selectable markers associated with the oep80-1 and oep80-2 insertions segregated abnormally, suggesting embryo lethality of the homozygous genotypes. Indeed, no homozygotes were identified among >100 individuals, and heterozygotes of both mutants produced approximately 25% aborted seeds upon self-pollination. Embryo arrest occurred at a relatively late stage (globular embryo proper) as revealed by analysis using Nomarski optics microscopy. This is substantially later than arrest caused by loss of the principal Toc75 isoform, atToc75-III (two-cell stage), suggesting a more specialized role for AtOEP80. Surprisingly, the oep80-3 T-DNA (located in exon 1 between the first and second ATG codons of the open reading frame) did not cause any detectable developmental defects or affect the size of the AtOEP80 protein in chloroplasts. This indicates that the N-terminal region of AtOEP80 is not essential for the targeting, biogenesis, or functionality of the protein, in contrast with atToc75-III, which requires a bipartite targeting sequence.
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