ArticlePloS one2010
The Mrs1 splicing factor binds the bI3 group I intron at each of two tetraloop-receptor motifs.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Watching ion-driven kinetics of ribozyme folding and misfolding caused by energetic and topological frustration one molecule at a time.Nucleic acids research · 2023Article
- Fuzzy RNA recognition by the Trypanosoma brucei editosome.Nucleic acids research · 2022Article
- A structural map of oncomiR-1 at single-nucleotide resolution.Nucleic acids research · 2017Article
- Exploring the electrostatic energy landscape for tetraloop-receptor docking.Physical chemistry chemical physics : PCCP · 2014Article
- Nuclear group I introns in self-splicing and beyond.Mobile DNA · 2013Article
- Three-dimensional RNA structure refinement by hydroxyl radical probing.Nature methods · 2012Article
- Exploring RNA structural codes with SHAPE chemistry.Accounts of chemical research · 2011Article
- Mne1 is a novel component of the mitochondrial splicing apparatus responsible for processing of a COX1 group I intron in yeast.The Journal of biological chemistry · 2011Article
- Multiple molecular mechanisms cause reproductive isolation between three yeast species.PLoS biology · 2010Article
- Nonhierarchical ribonucleoprotein assembly suggests a strain-propagation model for protein-facilitated RNA folding.Biochemistry · 2010Article
- Advances in RNA structure analysis by chemical probing.Current opinion in structural biology · 2010Review
- High-throughput SHAPE and hydroxyl radical analysis of RNA structure and ribonucleoprotein assembly.Methods in enzymology · 2009Article
- Article
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2 authors at 1 institution in 1 country.
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Abstract
Most large ribozymes require protein cofactors in order to function efficiently. The yeast mitochondrial bI3 group I intron requires two proteins for efficient splicing, Mrs1 and the bI3 maturase. Mrs1 has evolved from DNA junction resolvases to function as an RNA cofactor for at least two group I introns; however, the RNA binding site and the mechanism by which Mrs1 facilitates splicing were unknown. Here we use high-throughput RNA structure analysis to show that Mrs1 binds a ubiquitous RNA tertiary structure motif, the GNRA tetraloop-receptor interaction, at two sites in the bI3 RNA. Mrs1 also interacts at similar tetraloop-receptor elements, as well as other structures, in the self-folding Azoarcus group I intron and in the RNase P enzyme. Thus, Mrs1 recognizes general features found in the tetraloop-receptor motif. Identification of the two Mrs1 binding sites now makes it possible to create a model of the complete six-component bI3 ribonucleoprotein. All protein cofactors bind at the periphery of the RNA such that every long-range RNA tertiary interaction is stabilized by protein binding, involving either Mrs1 or the bI3 maturase. This work emphasizes the strong evolutionary pressure to bolster RNA tertiary structure with RNA-binding interactions as seen in the ribosome, spliceosome, and other large RNA machines.
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