ArticleMolecular biology of the cell2011
Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.
Article in Molecular biology of the cell, 2011. 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, 45 citations in OpenAlex.
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.Nature communications · 2022Article
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 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
- Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway.The protein journal · 2019Review
- 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
- YidC and SecYEG form a heterotetrameric protein translocation channel.Scientific reports · 2017Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.The Journal of cell biology · 2015Article
- Ribosome-SRP-FtsY cotranslational targeting complex in the closed state.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Dynamic interaction of the sec translocon with the chaperone PpiD.The Journal of biological chemistry · 2014Article
- Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting.The Journal of cell biology · 2014Article
- YlxM is a newly identified accessory protein that influences the function of signal recognition particle pathway components in Streptococcus mutans.Journal of bacteriology · 2014Article
- Signal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences.PloS one · 2014Article
- Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex.Nature structural & molecular biology · 2013Article
- SecYEG activates GTPases to drive the completion of cotranslational protein targeting.The Journal of cell biology · 2013Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein targeting by the signal recognition particle (SRP) and the bacterial SRP receptor FtsY requires a series of closely coordinated steps that monitor the presence of a substrate, the membrane, and a vacant translocon. Although the influence of substrate binding on FtsY-SRP complex formation is well documented, the contribution of the membrane is largely unknown. In the current study, we found that negatively charged phospholipids stimulate FtsY-SRP complex formation. Phospholipids act on a conserved positively charged amphipathic helix in FtsY and induce a conformational change that strongly enhances the FtsY-lipid interaction. This membrane-bound, signal sequence-independent FtsY-SRP complex is able to recruit RNCs to the membrane and to transfer them to the Sec translocon. Significantly, the same results were also observed with an artificial FtsY-SRP fusion protein, which was tethered to the membrane via a transmembrane domain. This indicates that substrate recognition by a soluble SRP is not essential for cotranslational targeting in Escherichia coli. Our findings reveal a remarkable flexibility of SRP-dependent protein targeting, as they indicate that substrate recognition can occur either in the cytosol via ribosome-bound SRP or at the membrane via a preassembled FtsY-SRP 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.