ArticleRNA (New York, N.Y.)2005
Structural insights into SRP RNA: an induced fit mechanism for SRP assembly.
Article in RNA (New York, N.Y.), 2005. 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
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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.
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.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Bridging technical innovation and computational advances in studies of RNA-protein assemblies.Nature reviews. Genetics · 2026Review
- RNA-protein interaction prediction without high-throughput data: An overview and benchmark ofComputational and structural biotechnology journal · 2024Article
- Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Footprinting SHAPE-eCLIP Reveals Transcriptome-wide Hydrogen Bonds at RNA-Protein Interfaces.Molecular cell · 2020Article
- How RNA-Binding Proteins Interact with RNA: Molecules and Mechanisms.Molecular cell · 2020Review
- 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
- Structural Changes of RNA in Complex with Proteins in the SRP.Frontiers in molecular biosciences · 2018Review
- The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Current microbiology · 2017Review
- ProbeAlign: incorporating high-throughput sequencing-based structure probing information into ncRNA homology search.BMC bioinformatics · 2014Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Compositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.Journal of molecular evolution · 2011Article
- Archaea signal recognition particle shows the way.Archaea (Vancouver, B.C.) · 2010Review
- Compositional properties and thermal adaptation of SRP-RNA in bacteria and archaea.Journal of molecular evolution · 2010Article
- Transposable elements in disease-associated cryptic exons.Human genetics · 2010Article
- Protein transport across and into cell membranes in bacteria and archaea.Cellular and molecular life sciences : CMLS · 2010Review
- Three-way RNA junctions with remote tertiary contacts: a recurrent and highly versatile fold.RNA (New York, N.Y.) · 2009Review
- Article
- Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- A threefold RNA-protein interface in the signal recognition particle gates native complex assembly.Journal of molecular biology · 2007Article
- Rearrangement of competing U2 RNA helices within the spliceosome promotes multiple steps in splicing.Genes & development · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proper assembly of large protein-RNA complexes requires sequential binding of the proteins to the RNA. The signal recognition particle (SRP) is a multiprotein-RNA complex responsible for the cotranslational targeting of proteins to biological membranes. Here we describe the crystal structure at 2.6-A resolution of the S-domain of SRP RNA from the archeon Methanococcus jannaschii. Comparison of this structure with the SRP19-bound form reveals the nature of the SRP19-induced conformational changes, which promote subsequent SRP54 attachment. These structural changes are initiated at the SRP19 binding site and transmitted through helix 6 to looped-out adenosines, which form tertiary RNA interaction with helix 8. Displacement of these adenosines enforces a conformational change of the asymmetric loop structure in helix 8. In free RNA, the three unpaired bases A195, C196, and C197 are directed toward the helical axis, whereas upon SRP19 binding the loop backbone inverts and the bases are splayed out in a conformation that resembles the SRP54-bound form. Nucleotides adjacent to the bulged nucleotides seem to be particularly important in the regulation of this loop transition. Binding of SRP19 to 7S RNA reveals an elegant mechanism of how protein-induced changes are directed through an RNA molecule and may relate to those regulating the assembly of other RNPs.
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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.