ArticleProceedings of the National Academy of Sciences of the United States of America1999
The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 180 citations in OpenAlex.
- Septin-mediated coupling of protein import and division during chloroplast evolution.bioRxiv : the preprint server for biology · 2026Article
- AnaToc75 (Alr2269) mediates calcium uptake across the outer membrane inJournal of bacteriology · 2025Article
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Cracking outer membrane biogenesis.Biochimica et biophysica acta. Molecular cell research · 2023Article
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- The Two TpsB-Like Proteins inJournal of bacteriology · 2021Article
- Coexpressed subunits of dual genetic origin define a conserved supercomplex mediating essential protein import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Origins, function, and regulation of the TOC-TIC general protein import machinery of plastids.Journal of experimental botany · 2020Article
- En route into chloroplasts: preproteins' way home.Photosynthesis research · 2018Review
- Evolution of protein transport to the chloroplast envelope membranes.Photosynthesis research · 2018Review
- Membrane integration of an essential β-barrel protein prerequires burial of an extracellular loop.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Characterization of a stalled complex on the β-barrel assembly machine.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Characterization of the β-barrel assembly machine accessory lipoproteins from Borrelia burgdorferi.BMC microbiology · 2015Article
- Evolution and targeting of Omp85 homologs in the chloroplast outer envelope membrane.Frontiers in plant science · 2014Article
- bam Lipoproteins Assemble BamA in vitro.Biochemistry · 2013Article
- 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
- Assembly of the β-Barrel Outer Membrane Proteins in Gram-Negative Bacteria, Mitochondria, and Chloroplasts.ISRN molecular biology · 2012Review
- From evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteria.International journal of molecular sciences · 2012Review
- A systematic screen to discover and analyze apicoplast proteins identifies a conserved and essential protein import factor.PLoS pathogens · 2011Article
- Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.EcoSal Plus · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The known envelope membrane proteins of the chloroplastic protein import apparatus lack sequence similarity to proteins of other eukaryotic or prokaryotic protein transport systems. However, we detected a putative homolog of the gene encoding Toc75, the protein-translocating channel from the outer envelope membrane of pea chloroplasts, in the genome of the cyanobacterium Synechocystis sp. PCC 6803. We investigated whether the low sequence identity of 21% reflects a structural and functional relationship between the two proteins. We provide evidence that the cyanobacterial protein is also localized in the outer membrane. From this information and the similarity of the predicted secondary structures, we conclude that Toc75 and the cyanobacterial protein, referred to as SynToc75, are structural homologs. synToc75 is essential, as homozygous null mutants were not recovered after directed mutagenesis. Sequence analysis indicates that SynToc75 belongs to a family of outer membrane proteins from Gram-negative bacteria whose function is not yet known. However, we demonstrate that these proteins are related to a specific group of prokaryotic secretion channels that transfer virulence factors, such as hemolysins and adhesins, across the outer membrane.
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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.