ArticleNature chemical biology2010
The 2'-OH group at the group II intron terminus acts as a proton shuttle.
Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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
9 citing papers in PubMed.
- Fluorogenic RNA Aptamer-Based Activity Quantification of T7 RNA Polymerase.Biochemistry · 2026Article
- A revised mechanism for (p)ppGpp synthesis by Rel proteins: The critical role of the 2'-OH of GTP.The Journal of biological chemistry · 2020Article
- Retroelement origins of pre-mRNA splicing.Wiley interdisciplinary reviews. RNA · 2020Review
- Visualizing group II intron dynamics between the first and second steps of splicing.Nature communications · 2020Article
- Article
- Phosphodiester models for cleavage of nucleic acids.Beilstein journal of organic chemistry · 2018Review
- Theoretical Analysis of a Self-Replicator With Reduced Template Inhibition Based on an Informational Leaving Group.Journal of molecular evolution · 2016Article
- Article
- Crystal structure of a group II intron in the pre-catalytic state.Nature structural & molecular biology · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Group II introns are self-splicing ribozymes that excise themselves from precursor RNAs and catalyze the joining of flanking exons. Excised introns can behave as parasitic RNA molecules: they can catalyze their own insertion into DNA and RNA via a reverse splicing reaction. Previous studies have identified mechanistic roles for various functional groups located in the catalytic core of the intron and within target molecules. Here we introduce a new method for synthesizing long RNA molecules with a modified nucleotide at the 3' terminus. This modification allows us to examine the mechanistic role of functional groups adjacent to the reaction nucleophile. During reverse splicing, the 3'-OH group of the intron terminus attacks the phosphodiester linkage of spliced exon sequences. Here we show that the adjacent 2'-OH group on the intron terminus plays an essential role in activating the nucleophile by stripping away a proton from the 3'-OH and then shuttling it from the active site.
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Registered trials
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