ArticleScience (New York, N.Y.)2009
Signal sequences activate the catalytic switch of SRP RNA.
Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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
47 citing papers in PubMed, 76 citations in OpenAlex.
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022Review
- Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.Nature communications · 2022Article
- Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle.Cell reports · 2021Article
- Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.Journal of bacteriology · 2020Article
- Signal Recognition Particle RNA Contributes to Oxidative Stress Response inFrontiers in microbiology · 2020Article
- Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- The Host RNAs in Retroviral Particles.Viruses · 2016Review
- Dynamics of co-translational protein targeting.Current opinion in chemical biology · 2015Review
- Signal-sequence induced conformational changes in the signal recognition particle.Nature communications · 2015Article
- Allosteric response and substrate sensitivity in peptide binding of the signal recognition particle.The Journal of biological chemistry · 2014Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Signal recognition particle-ribosome binding is sensitive to nascent chain length.The Journal of biological chemistry · 2014Article
- Fidelity of cotranslational protein targeting by the signal recognition particle.Annual review of biophysics · 2014Review
- The structural basis of FtsY recruitment and GTPase activation by SRP RNA.Molecular cell · 2013Article
- Structural insights of non-canonical U*U pair and Hoogsteen interaction probed with Se atom.Nucleic acids research · 2013Article
- Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex.Nature structural & molecular biology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The signal recognition particle (SRP) recognizes polypeptide chains bearing a signal sequence as they emerge from the ribosome, and then binds its membrane-associated receptor (SR), thereby delivering the ribosome-nascent chain complex to the endoplasmic reticulum in eukaryotic cells and the plasma membrane in prokaryotic cells. SRP RNA catalytically accelerates the interaction of SRP and SR, which stimulates their guanosine triphosphatase (GTPase) activities, leading to dissociation of the complex. We found that although the catalytic activity of SRP RNA appeared to be constitutive, SRP RNA accelerated complex formation only when SRP was bound to a signal sequence. This crucial control step was obscured because a detergent commonly included in the reaction buffer acted as a signal peptide mimic. Thus, SRP RNA is a molecular switch that renders the SRP-SR GTPase engine responsive to signal peptide recruitment, coupling GTP hydrolysis to productive protein targeting.
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.