ArticleThe Journal of biological chemistry2010
Conserved negative charges in the transmembrane segments of subunit K of the NADH:ubiquinone oxidoreductase determine its dependence on YidC for membrane insertion.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 46 citations in OpenAlex.
- Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.The EMBO journal · 2026Article
- A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024Review
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- Fates of Sec, Tat, and YidC Translocases in Mitochondria and Other Eukaryotic Compartments.Molecular biology and evolution · 2021Review
- Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Celecoxib Derivative Eradicates Antibiotic-ResistantInternational journal of molecular sciences · 2020Article
- The WRB Subunit of the Get3 Receptor is Required for the Correct Integration of its Partner CAML into the ER.Scientific reports · 2019Article
- The Conserved Role of YidC in Membrane Protein Biogenesis.Microbiology spectrum · 2019Article
- Sec translocon has an insertase-like function in addition to polypeptide conduction through the channel.F1000Research · 2019Review
- A Bacterial Stress Response Regulates Respiratory Protein Complexes To Control Envelope Stress Adaptation.Journal of bacteriology · 2017Article
- Role of the Cytosolic Loop C2 and the C Terminus of YidC in Ribosome Binding and Insertion Activity.The Journal of biological chemistry · 2015Article
- YidC/Alb3/Oxa1 Family of Insertases.The Journal of biological chemistry · 2015Review
- Hydrophilic microenvironment required for the channel-independent insertase function of YidC protein.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015Review
- Article
- Charge composition features of model single-span membrane proteins that determine selection of YidC and SecYEG translocase pathways in Escherichia coli.The Journal of biological chemistry · 2013Article
- Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle.Molecular biology of the cell · 2012Article
- Activators of the glutamate-dependent acid resistance system alleviate deleterious effects of YidC depletion in Escherichia coli.Journal of bacteriology · 2011Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All members of the Oxa1/Alb3/YidC family have been implicated in the biogenesis of respiratory and energy transducing proteins. In Escherichia coli, YidC functions together with and independently of the Sec system. Although the range of proteins shown to be dependent on YidC continues to increase, the exact role of YidC in insertion remains enigmatic. Here we show that YidC is essential for the insertion of subunit K of the NADH:ubiquinone oxidoreductase and that the dependence is due to the presence of two conserved glutamate residues in the transmembrane segments of subunit K. The results suggest a model in which YidC serves as a membrane chaperone for the insertion of the less hydrophobic, negatively charged transmembrane segments of NuoK.
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.