ArticleRNA (New York, N.Y.)2011
Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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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.
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Who cites it
21 citing papers in PubMed.
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.Science advances · 2021Article
- A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting.The Journal of cell biology · 2019Article
- 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
- Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The Journal of biological chemistry · 2017Article
- Co-evolution of Two GTPases Enables Efficient Protein Targeting in an RNA-less Chloroplast Signal Recognition Particle Pathway.The Journal of biological chemistry · 2017Article
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions.Nature structural & molecular biology · 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
- Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting.The Journal of cell biology · 2014Article
- Fidelity of cotranslational protein targeting by the signal recognition particle.Annual review of biophysics · 2014Review
- Molecular mechanism of GTPase activation at the signal recognition particle (SRP) RNA distal end.The Journal of biological chemistry · 2013Article
- Fingerloop activates cargo delivery and unloading during cotranslational protein targeting.Molecular biology of the cell · 2013Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Activated GTPase movement on an RNA scaffold drives co-translational protein targeting.Nature · 2012Article
- Dynamic switch of the signal recognition particle from scanning to targeting.Nature structural & molecular biology · 2012Article
- Translation elongation regulates substrate selection by the signal recognition particle.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
During cotranslational protein targeting by the Signal Recognition Particle (SRP), the correct cargo accelerates stable complex assembly between the SRP and SRP receptor (FtsY) by several orders of magnitude, thus enabling rapid and faithful cargo delivery to the target membrane. The molecular mechanism underlying this cargo-induced rate acceleration has been unclear. Here we show that the SRP RNA allows assembly of the SRP-FtsY complex to be specifically stimulated by a correct cargo, and, reciprocally, a correct cargo enables the SRP RNA to optimize its electrostatic interactions with FtsY. These results combined with recent structural work led us to suggest a "conformational selection" model that explains the synergistic action of the SRP RNA with the cargo in accelerating complex assembly. In addition to its previously proposed role in preventing the premature dissociation of SRP and FtsY, we found that the SRP RNA also plays an active role in ensuring the formation of productive assembly intermediates, thus guiding the SRP and FtsY through the most efficient pathway of assembly.
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Registered trials
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