ArticleRNA (New York, N.Y.)2005
The snRNP 15.5K protein folds its cognate K-turn RNA: a combined theoretical and biochemical study.
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 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Connecting genotype and phenotype in minor spliceosome diseases.RNA (New York, N.Y.) · 2025Review
- SlRBP1 promotes translational efficiency via SleIF4A2 to maintain chloroplast function in tomato.The Plant cell · 2022Article
- RNA kink-turns are highly anisotropic with respect to lateral displacement of the flanking stems.Biophysical journal · 2022Article
- RNA Structural Dynamics As Captured by Molecular Simulations: A Comprehensive Overview.Chemical reviews · 2018Review
- Cross-species conservation of complementary amino acid-ribonucleobase interactions and their potential for ribosome-free encoding.Scientific reports · 2015Article
- RNA structure determination by solid-state NMR spectroscopy.Nature communications · 2015Article
- Biochemical defects in minor spliceosome function in the developmental disorder MOPD I.RNA (New York, N.Y.) · 2014Article
- Interactions of noncanonical motifs with hnRNP A2 promote activity-dependent RNA transport in neurons.The Journal of cell biology · 2014Article
- Structural basis for the dual U4 and U4atac snRNA-binding specificity of spliceosomal protein hPrp31.RNA (New York, N.Y.) · 2011Article
- Spatial code recognition in neuronal RNA targeting: role of RNA-hnRNP A2 interactions.The Journal of cell biology · 2011Article
- Structure of the K-turn U4 RNA: a combined NMR and SANS study.Nucleic acids research · 2010Article
- Plasticity of the RNA kink turn structural motif.RNA (New York, N.Y.) · 2010Article
- Elbow flexibility of the kt38 RNA kink-turn motif investigated by free-energy molecular dynamics simulations.Biophysical journal · 2009Article
- Dynamic guide-target interactions contribute to sequential 2'-O-methylation by a unique archaeal dual guide box C/D sRNP.RNA (New York, N.Y.) · 2008Article
- Conformations of flanking bases in HIV-1 RNA DIS kissing complexes studied by molecular dynamics.Biophysical journal · 2007Article
- Analysis of sequence and structural features that identify the B/C motif of U3 small nucleolar RNA as the recognition site for the Snu13p-Rrp9p protein pair.Molecular and cellular biology · 2007Article
- Elastic properties of ribosomal RNA building blocks: molecular dynamics of the GTPase-associated center rRNA.Nucleic acids research · 2007Article
- Consecutive GA pairs stabilize medium-size RNA internal loops.Biochemistry · 2006Article
- Conformational dynamics of RNA-peptide binding: a molecular dynamics simulation study.Biophysical journal · 2006Article
- Molecular dynamics simulations of sarcin-ricin rRNA motif.Nucleic acids research · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human 15.5K protein binds to the 5' stem-loop of U4 snRNA, promotes the assembly of the spliceosomal U4/U6 snRNP, and is required for the recruitment of the 61K protein and the 20/60/90K protein complex to the U4 snRNA. In the crystallographic structure of the 15.5K-U4 snRNA complex, the conformation of the RNA corresponds to the family of kink-turn (K-turn) structural motifs. We simulated the complex and the free RNA, showing how the protein binding and the intrinsic flexibility contribute to the RNA folding process. We found that the RNA is significantly more flexible in the absence of the 15.5K protein. Conformational transitions such as the interconversion between alternative purine stacking schemes, the loss of G-A base pairs, and the opening of the K-turn occur only in the free RNA. Furthermore, the stability of one canonical G-C base pair is influenced both by the binding of the 15.5K protein and the nature of the adjacent structural element in the RNA. We performed chemical RNA modification experiments and observed that the free RNA lacks secondary structure elements, a result in excellent agreement with the simulations. Based on these observations, we propose a protein-assisted RNA folding mechanism in which the RNA intrinsic flexibility functions as a catalyst.
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