ArticleNucleic acids research1999
Presence of a coordinated metal ion in a trans-acting antigenomic delta ribozyme.
Article in Nucleic acids research, 1999. 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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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Characterization of the trans Watson-Crick GU base pair located in the catalytic core of the antigenomic HDV ribozyme.PloS one · 2012Article
- A novel structural rearrangement of hepatitis delta virus antigenomic ribozyme.Nucleic acids research · 2007Article
- Cations and hydration in catalytic RNA: molecular dynamics of the hepatitis delta virus ribozyme.Biophysical journal · 2006Article
- Cross-linking experiments reveal the presence of novel structural features between a hepatitis delta virus ribozyme and its substrate.RNA (New York, N.Y.) · 2004Article
- Ribozyme-based gene-inactivation systems require a fine comprehension of their substrate specificities; the case of delta ribozyme.Current medicinal chemistry · 2003Article
- Formation of the P1.1 pseudoknot is critical for both the cleavage activity and substrate specificity of an antigenomic trans-acting hepatitis delta ribozyme.Nucleic acids research · 2003Article
- Kinetic and binding analysis of the catalytic involvement of ribose moieties of a trans-acting delta ribozyme.The Journal of biological chemistry · 2002Article
- Imino proton NMR analysis of HDV ribozymes: nested double pseudoknot structure and Mg2+ ion-binding site close to the catalytic core in solution.Nucleic acids research · 2002Article
- Catalytic cleavage of cis- and trans-acting antigenomic delta ribozymes in the presence of various divalent metal ions.Nucleic acids research · 2001Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have investigated the cleavage induced by metal ions in an antigenomic form of a trans-acting delta ribozyme. A specific Mg(2+)-induced cleavage at position G(52)at the bottom of the P2 stem was observed to occur solely within catalytically active ribozyme-substrate complexes (i.e. those that performed the essential conformational transition step). Only the divalent cations which support catalytic activity permitted the detection of specific induced cleavages in this region. Using various mutant ribozymes and substrates, we demonstrated a correlation between enzymatic activity and the Mg(2+)-induced cleavage pattern. We show that the efficiency of the coordination of the magnesium to its binding site is related to the nature of the base pair in the middle of the P1 stem (i.e. Rz(23)-S(8)). Together with additional evidence from nuclease probing experiments that indicates the occurrence of a structural rearrangement involving the bottom of the P2 stem upon formation of the P1 helix, these results show that an intimate relationship exists between the folding and the catalytic activity of the delta ribozyme.
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