ArticleProceedings of the National Academy of Sciences of the United States of America2011
Chloroplast Omp85 proteins change orientation during evolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 89 citations in OpenAlex.
- Review
- Converting antimicrobial into targeting peptides reveals key features governing protein import into mitochondria and chloroplasts.Plant communications · 2023Article
- 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
- The role of antimicrobial peptides in the evolution of endosymbiotic protein import.PLoS pathogens · 2021Article
- Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.Journal of bacteriology · 2020Article
- The gain-of-function alleleProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Evidence Supporting an Antimicrobial Origin of Targeting Peptides to Endosymbiotic Organelles.Cells · 2020Article
- 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
- Chloroplast Outer Membrane β-Barrel Proteins Use Components of the General Import Apparatus.The Plant cell · 2019Article
- Co-orthologues of ribosome biogenesis factors in A. thaliana are differentially regulated by transcription factors.Plant cell reports · 2019Article
- Plant-specific ribosome biogenesis factors in Arabidopsis thaliana with essential function in rRNA processing.Nucleic acids research · 2019Article
- Evolution of protein transport to the chloroplast envelope membranes.Photosynthesis research · 2018Review
- Late ribosomal protein localization inFEBS open bio · 2018Article
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms.Frontiers in plant science · 2017Review
- Nucleolar Proteome Analysis and Proteasomal Activity Assays Reveal a Link between Nucleolus and 26S Proteasome inFrontiers in plant science · 2017Article
- Polypeptide Transport-Associated Domains of the Toc75 Channel Protein Are Located in the Intermembrane Space of Chloroplasts.Plant physiology · 2016Article
- Characterization of the targeting signal in mitochondrial β-barrel proteins.Nature communications · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of outer membrane proteins (OMPs) from gram-negative bacteria and many of mitochondria and chloroplasts are β-barrels. Insertion and assembly of these proteins are catalyzed by the Omp85 protein family in a seemingly conserved process. All members of this family exhibit a characteristic N-terminal polypeptide-transport-associated (POTRA) and a C-terminal 16-stranded β-barrel domain. In plants, two phylogenetically distinct and essential Omp85's exist in the chloroplast outer membrane, namely Toc75-III and Toc75-V. Whereas Toc75-V, similar to the mitochondrial Sam50, is thought to possess the original bacterial function, its homolog, Toc75-III, evolved to the pore-forming unit of the TOC translocon for preprotein import. In all current models of OMP biogenesis and preprotein translocation, a topology of Omp85 with the POTRA domain in the periplasm or intermembrane space is assumed. Using self-assembly GFP-based in vivo experiments and in situ topology studies by electron cryotomography, we show that the POTRA domains of both Toc75-III and Toc75-V are exposed to the cytoplasm. This unexpected finding explains many experimental observations and requires a reevaluation of current models of OMP biogenesis and TOC complex function.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.