ArticleThe Journal of cell biology2015
Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.
Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 49 citations in OpenAlex.
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- The inhibitory mechanism of a small protein reveals its role in antimicrobial peptide sensing.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- 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
- Antibiotic Drug screening and Image Characterization Toolbox (A.D.I.C.T.): a robust imaging workflow to monitor antibiotic stress response in bacterial cellsF1000Research · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Scientific reports · 2020Article
- Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome inThe Journal of biological chemistry · 2019Article
- Ribosome-Associated Chloroplast SRP54 Enables Efficient Cotranslational Membrane Insertion of Key Photosynthetic Proteins.The Plant cell · 2019Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.Protein science : a publication of the Protein Society · 2019Review
- Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway.The protein journal · 2019Review
- Mutagenesis of DsbAss is Crucial for the Signal Recognition Particle Mechanism inBiomolecules · 2019Article
- Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon.Scientific reports · 2018Article
- The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY.Scientific reports · 2018Article
- Article
- Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Nature communications · 2017Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Current microbiology · 2017Review
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cotranslational protein targeting delivers proteins to the bacterial cytoplasmic membrane or to the eukaryotic endoplasmic reticulum membrane. The signal recognition particle (SRP) binds to signal sequences emerging from the ribosomal tunnel and targets the ribosome-nascent-chain complex (RNC) to the SRP receptor, termed FtsY in bacteria. FtsY interacts with the fifth cytosolic loop of SecY in the SecYEG translocon, but the functional role of the interaction is unclear. By using photo-cross-linking and fluorescence resonance energy transfer measurements, we show that FtsY-SecY complex formation is guanosine triphosphate independent but requires a phospholipid environment. Binding of an SRP-RNC complex exposing a hydrophobic transmembrane segment induces a rearrangement of the SecY-FtsY complex, which allows the subsequent contact between SecY and ribosomal protein uL23. These results suggest that direct RNC transfer to the translocon is guided by the interaction between SRP and translocon-bound FtsY in a quaternary targeting complex.
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.