ArticleNucleic acids research2007
Use of a novel Förster resonance energy transfer method to identify locations of site-bound metal ions in the U2-U6 snRNA complex.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Mechanistic insights into 50Science advances · 2025Article
- Structural and functional studies of SF1B Pif1 from Thermus oshimai reveal dimerization-induced helicase inhibition.Nucleic acids research · 2021Article
- Role of the central junction in folding topology of the protein-free human U2-U6 snRNA complex.RNA (New York, N.Y.) · 2020Article
- Article
- A High-Throughput Assay for Developing Inhibitors of PhoP, a Virulence Factor of Mycobacterium tuberculosis.Combinatorial chemistry & high throughput screening · 2016Article
- Conformational heterogeneity of the protein-free human spliceosomal U2-U6 snRNA complex.RNA (New York, N.Y.) · 2013Article
- Probing nucleic acid interactions and pre-mRNA splicing by Förster Resonance Energy Transfer (FRET) microscopy.International journal of molecular sciences · 2012Review
- Evolutionarily divergent spliceosomal snRNAs and a conserved non-coding RNA processing motif in Giardia lamblia.Nucleic acids research · 2012Article
- Metal binding and substrate positioning by evolutionarily invariant U6 sequences in catalytically active protein-free snRNAs.RNA (New York, N.Y.) · 2010Article
- Single-molecule analysis of protein-free U2-U6 snRNAs.Nature structural & molecular biology · 2009Article
- Identification of catalytic metal ion ligands in ribozymes.Methods (San Diego, Calif.) · 2009Review
- Computational identification of four spliceosomal snRNAs from the deep-branching eukaryote Giardia intestinalis.PloS one · 2008Article
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Authors and funding
6 authors.
Funding
Abstract
U2 and U6 snRNAs pair to form a phylogenetically conserved complex at the catalytic core of the spliceosome. Interactions with divalent metal ions, particularly Mg(II), at specific sites are essential for its folding and catalytic activity. We used a novel Förster resonance energy transfer (FRET) method between site-bound luminescent lanthanide ions and a covalently attached fluorescent dye, combined with supporting stoichiometric and mutational studies, to determine locations of site-bound Tb(III) within the human U2-U6 complex. At pH 7.2, we detected three metal-ion-binding sites in: (1) the consensus ACACAGA sequence, which forms the internal loop between helices I and III; (2) the four-way junction, which contains the conserved AGC triad; and (3) the internal loop of the U6 intra-molecular stem loop (ISL). Binding at each of these sites is supported by previous phosphorothioate substitution studies and, in the case of the ISL site, by NMR. Binding of Tb(III) at the four-way junction and the ISL sites was found to be pH-dependent, with no ion binding observed below pH 6 and 7, respectively. This pH dependence of metal ion binding suggests that the local environment may play a role in the binding of metal ions, which may impact on splicing activity.
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