ArticleNucleic acids research2000
Structure-function relationships of two closely related group IC3 intron ribozymes from Azoarcus and Synechococcus pre-tRNA.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- In vitro selected GUAA tetraloop-binding receptors with structural plasticity and evolvability towards natural RNA structural modules.Nucleic acids research · 2021Article
- Article
- A kinetic and thermodynamic framework for the Azoarcus group I ribozyme reaction.RNA (New York, N.Y.) · 2014Article
- Bacterial group I introns: mobile RNA catalysts.Mobile DNA · 2014Article
- Article
- Rational optimization of the DSL ligase ribozyme with GNRA/receptor interacting modules.Archives of biochemistry and biophysics · 2009Article
- One RNA plays three roles to provide catalytic activity to a group I intron lacking an endogenous internal guide sequence.Nucleic acids research · 2009Article
- Comprehensive features of natural and in vitro selected GNRA tetraloop-binding receptors.Nucleic acids research · 2008Article
- Tertiary interactions determine the accuracy of RNA folding.Journal of the American Chemical Society · 2008Article
- Long-term evolution of the S788 fungal nuclear small subunit rRNA group I introns.RNA (New York, N.Y.) · 2004Article
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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 two group IC3 pre-tRNA introns from Azoarcus and Synechococcus share very analogous secondary structures. They are small group I ribozymes that possess only two peripheral domains, P2 and P9. However, the 3'-splice site hydrolysis activity of the Synechococcus ribozyme critically depends on P2 whereas that of Azoarcus does not, indicating that the structure-function relationships of the two ribozymes are strikingly different despite their structural resemblance. To identify the element(s) that determines the catalytic properties of these ribozymes, we undertook analyses of chimeric ribozymes prepared by swapping their structural elements. We found that the difference can be attributed to a small number of nucleotides within the conserved core region. Further analysis by employing in vitro selection revealed that a base triple interaction (P4bp3 x J6/7-2) is a critical element for determining activity and suggests the existence of a novel base quintuple involving the base triple P4bp5 x J8/7-5.
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