ArticleThe Journal of biological chemistry2013
Molecular mechanism of GTPase activation at the signal recognition particle (SRP) RNA distal end.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- The phenotypic landscape of the model firmicuteProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.Science advances · 2021Article
- Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions.Nucleic acids research · 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
- Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Nature communications · 2017Article
- The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Current microbiology · 2017Review
- Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.Nucleic acids research · 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
- Structural conservation in the template/pseudoknot domain of vertebrate telomerase RNA from teleost fish to human.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Analyzing Single-Molecule Protein Transportation Experiments via Hierarchical Hidden Markov Models.Journal of the American Statistical Association · 2016Article
- Dynamics of co-translational protein targeting.Current opinion in chemical biology · 2015Review
- The completed genome sequence of the pathogenic ascomycete fungus Fusarium graminearum.BMC genomics · 2015Article
- Signal recognition particle-ribosome binding is sensitive to nascent chain length.The Journal of biological chemistry · 2014Article
- RNA gymnastics in mammalian signal recognition particle assembly.RNA biology · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The signal recognition particle (SRP) RNA is a universally conserved and essential component of the SRP that mediates the co-translational targeting of proteins to the correct cellular membrane. During the targeting reaction, two functional ends in the SRP RNA mediate distinct functions. Whereas the RNA tetraloop facilitates initial assembly of two GTPases between the SRP and SRP receptor, this GTPase complex subsequently relocalizes ∼100 Å to the 5',3'-distal end of the RNA, a conformation crucial for GTPase activation and cargo handover. Here we combined biochemical, single molecule, and NMR studies to investigate the molecular mechanism of this large scale conformational change. We show that two independent sites contribute to the interaction of the GTPase complex with the SRP RNA distal end. Loop E plays a crucial role in the precise positioning of the GTPase complex on these two sites by inducing a defined bend in the RNA helix and thus generating a preorganized recognition surface. GTPase docking can be uncoupled from its subsequent activation, which is mediated by conserved bases in the next internal loop. These results, combined with recent structural work, elucidate how the SRP RNA induces GTPase relocalization and activation at the end of the protein targeting reaction.
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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.