ArticleJournal of molecular biology2010
Structure of a conserved retroviral RNA packaging element by NMR spectroscopy and cryo-electron tomography.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 66 citations in OpenAlex.
- Application of NMR to Large RNAs.Journal of molecular biology · 2025Review
- Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Identification of a putative Gag binding site critical for feline immunodeficiency virus genomic RNA packaging.RNA (New York, N.Y.) · 2023Article
- RNA structure determination: From 2D to 3D.Fundamental research · 2023Review
- Article
- NMR Studies of Retroviral Genome Packaging.Viruses · 2020Review
- Structural Insights into RNA Dimerization: Motifs, Interfaces and Functions.Molecules (Basel, Switzerland) · 2020Review
- A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Advances that facilitate the study of large RNA structure and dynamics by nuclear magnetic resonance spectroscopy.Wiley interdisciplinary reviews. RNA · 2019Review
- Review
- Retroviral Gag protein-RNA interactions: Implications for specific genomic RNA packaging and virion assembly.Seminars in cell & developmental biology · 2019Review
- Long-Range RNA Structural Information via a Paramagnetically Tagged Reporter Protein.Journal of the American Chemical Society · 2019Article
- Challenges and approaches to predicting RNA with multiple functional structures.RNA (New York, N.Y.) · 2018Review
- Isotope labeling for studying RNA by solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- Accurate Measurement of Residual Dipolar Couplings in Large RNAs by Variable Flip Angle NMR.Journal of the American Chemical Society · 2018Article
- Surprising Sequence Effects on GU Closure of Symmetric 2 × 2 Nucleotide RNA Internal Loops.Biochemistry · 2018Article
- Structure of the 30 kDa HIV-1 RNA Dimerization Signal by a Hybrid Cryo-EM, NMR, and Molecular Dynamics Approach.Structure (London, England : 1993) · 2018Article
- Retroviral RNA Dimerization: From Structure to Functions.Frontiers in microbiology · 2018Review
- Combining asymmetric 13C-labeling and isotopic filter/edit NOESY: a novel strategy for rapid and logical RNA resonance assignment.Nucleic acids research · 2017Article
- Applications of NMR to structure determination of RNAs large and small.Archives of biochemistry and biophysics · 2017Review
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
Abstract
The 5'-untranslated regions of all gammaretroviruses contain a conserved "double-hairpin motif" (Ψ(CD)) that is required for genome packaging. Both hairpins (SL-C and SL-D) contain GACG tetraloops that, in isolated RNAs, are capable of forming "kissing" interactions stabilized by two intermolecular G-C base pairs. We have determined the three-dimensional structure of the double hairpin from the Moloney murine leukemia virus ([Ψ(CD)](2), 132 nt, 42.8 kDa) using a (2)H-edited NMR-spectroscopy-based approach. This approach enabled the detection of (1)H-(1)H dipolar interactions that were not observed in previous studies of isolated SL-C and SL-D hairpin RNAs using traditional (1)H-(1)H correlated and (1)H-(13)C-edited NMR methods. The hairpins participate in intermolecular cross-kissing interactions (SL-C to SL-D' and SLC' to SL-D) and stack in an end-to-end manner (SL-C to SL-D and SL-C' to SL-D') that gives rise to an elongated overall shape (ca 95 Å×45 Å×25 Å). The global structure was confirmed by cryo-electron tomography (cryo-ET), making [Ψ(CD)](2) simultaneously the smallest RNA to be structurally characterized to date by cryo-ET and among the largest to be determined by NMR. Our findings suggest that, in addition to promoting dimerization, [Ψ(CD)](2) functions as a scaffold that helps initiate virus assembly by exposing a cluster of conserved UCUG elements for binding to the cognate nucleocapsid domains of assembling viral Gag proteins.
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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.