ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2018
Specific phosphorothioate substitution within domain 6 of a group II intron ribozyme leads to changes in local structure and metal ion binding.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 11 citations in OpenAlex.
- Metallo-herb complexes as emerging therapeutics: chemistry, synthesis approaches, and pharmacological insights.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Review
- The use of multiple liquid chromatography methods augmented by phosphorus-31 nuclear magnetic resonance to characterize the diastereomer composition in synthetic oligonucleotides.Journal of chromatography. A · 2026Article
- Structural Fingerprinting of Antisense Oligonucleotide Therapeutics by Solution NMR Spectroscopy.Pharmaceutical research · 2023Article
- Structural Fingerprinting of siRNA Therapeutics by Solution NMR Spectroscopy.Nucleic acid therapeutics · 2022Article
- Branch site bulge conformations in domain 6 determine functional sugar puckers in group II intron splicing.Nucleic acids research · 2019Article
- Celebrating Helmut Sigel.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
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5 authors at 2 institutions in 2 countries.
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Abstract
Group II introns are large self-splicing ribozymes that require high amounts of monovalent and divalent metal ions for folding and catalysis under in vitro conditions. Domain 6 of these ribozymes contains a highly conserved adenosine whose 2'-OH acts as a nucleophile during self-cleavage via the branching pathway. We have previously suggested a divalent metal ion that binds to the major groove at the GU wobble pair above the branch-A in a minimal, but active branch domain construct (D6-27) from the yeast mitochondrial intron Sc.ai5γ. Here we characterize metal ion binding to the phosphate oxygens at the branch site. In vitro transcription yielded a D6-27 construct where all R
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