ArticleJournal of molecular biology2008
Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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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
48 citing papers in PubMed.
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Heterogeneous folding landscapes and predetermined breaking points within a protein family.Protein science : a publication of the Protein Society · 2024Article
- Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting.The Journal of cell biology · 2019Article
- Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway.The protein journal · 2019Review
- Transcriptome analysis reveals an important candidate gene involved in both nodal metastasis and prognosis in lung adenocarcinoma.Cell & bioscience · 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
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- 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
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- Analyzing Single-Molecule Protein Transportation Experiments via Hierarchical Hidden Markov Models.Journal of the American Statistical Association · 2016Article
- Article
- Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Signal-sequence induced conformational changes in the signal recognition particle.Nature communications · 2015Article
- Identification and in silico analysis of helical lipid binding regions in proteins belonging to the amphitropic protein family.Journal of biosciences · 2014Article
- Real-time observation of signal recognition particle binding to actively translating ribosomes.eLife · 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
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Two GTPases in the signal recognition particle (SRP) and its receptor (SR) control the delivery of newly synthesized proteins to the endoplasmic reticulum or plasma membrane. During the protein targeting reaction, the 4.5S SRP RNA accelerates the association between the two GTPases by 400-fold. Using fluorescence resonance energy transfer, we demonstrate here that formation of a stable SRP x SR complex involves two distinct steps: a fast initial association between SRP and SR to form a GTP-independent early complex and then a GTP-dependent conformational rearrangement to form the stable final complex. We also found that the 4.5S SRP RNA significantly stabilizes the early GTP-independent intermediate. Furthermore, mutational analyses show that there is a strong correlation between the ability of the mutant SRP RNAs to stabilize the early intermediate and their ability to accelerate SRP x SR complex formation. We propose that the SRP RNA, by stabilizing the early intermediate, can give this transient intermediate a longer life time and therefore a higher probability to rearrange to the stable final complex. This provides a coherent model that explains how the 4.5S RNA exerts its catalytic role in SRP x SR complex assembly.
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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.