ArticleThe EMBO journal2008
Molecular modelling of the GIR1 branching ribozyme gives new insight into evolution of structurally related ribozymes.
Article in The EMBO journal, 2008. 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.
- Progress toward SHAPE Constrained Computational Prediction of Tertiary Interactions in RNA Structure.Non-coding RNA · 2021Article
- RNA-Puzzles Round II: assessment of RNA structure prediction programs applied to three large RNA structures.RNA (New York, N.Y.) · 2015Article
- Speciation of a group I intron into a lariat capping ribozyme.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Molecular characterization of a new member of the lariat capping twin-ribozyme introns.Mobile DNA · 2014Article
- Nuclear group I introns in self-splicing and beyond.Mobile DNA · 2013Article
- The role of robustness in phenotypic adaptation and innovation.Proceedings. Biological sciences · 2012Review
- RNase P: at last, the key finds its lock.RNA (New York, N.Y.) · 2011Article
- Dual-channel single-molecule fluorescence resonance energy transfer to establish distance parameters for RNA nanoparticles.ACS nano · 2010Article
- A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA.RNA (New York, N.Y.) · 2009Article
- A natural ribozyme with 3',5' RNA ligase activity.Nature chemical biology · 2009Article
- A structural basis for the recognition of 2'-deoxyguanosine by the purine riboswitch.Journal of molecular biology · 2009Article
- Toward predicting self-splicing and protein-facilitated splicing of group I introns.RNA (New York, N.Y.) · 2008Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Twin-ribozyme introns contain a branching ribozyme (GIR1) followed by a homing endonuclease (HE) encoding sequence embedded in a peripheral domain of a group I splicing ribozyme (GIR2). GIR1 catalyses the formation of a lariat with 3 nt in the loop, which caps the HE mRNA. GIR1 is structurally related to group I ribozymes raising the question about how two closely related ribozymes can carry out very different reactions. Modelling of GIR1 based on new biochemical and mutational data shows an extended substrate domain containing a GoU pair distinct from the nucleophilic residue that dock onto a catalytic core showing a different topology from that of group I ribozymes. The differences include a core J8/7 region that has been reduced and is complemented by residues from the pre-lariat fold. These findings provide the basis for an evolutionary mechanism that accounts for the change from group I splicing ribozyme to the branching GIR1 architecture. Such an evolutionary mechanism can be applied to other large RNAs such as the ribonuclease P.
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