ArticleNucleic acids research2004
Importance in catalysis of a magnesium ion with very low affinity for a hammerhead ribozyme.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Hammerhead ribozymes directed against mRNA of an essential gene inhibitFrontiers in microbiology · 2025Article
- Article
- Prebiotic Factors Influencing the Activity of a Ligase Ribozyme.Life (Basel, Switzerland) · 2017Article
- Catalytic diversity of extended hammerhead ribozymes.Biochemistry · 2008Article
- Role of Mg2+ in hammerhead ribozyme catalysis from molecular simulation.Journal of the American Chemical Society · 2008Article
- Coupling of fast and slow modes in the reaction pathway of the minimal hammerhead ribozyme cleavage.Biophysical journal · 2007Article
- Insight into the role of Mg in hammerhead ribozyme catalysis from X-ray crystallography and molecular dynamics simulation.Journal of chemical theory and computation · 2007Article
- Artificial tertiary motifs stabilize trans-cleaving hammerhead ribozymes under conditions of submillimolar divalent ions and high temperatures.RNA (New York, N.Y.) · 2004Article
Corrections and comments
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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
Available evidence suggests that Mg2+ ions are involved in reactions catalyzed by hammerhead ribozymes. However, the activity in the presence of exclusively monovalent ions led us to question whether divalent metal ions really function as catalysts when they are present. We investigated ribozyme activity in the presence of high levels of Mg2+ ions and the effects of Li+ ions in promoting ribozyme activity. We found that catalytic activity increased linearly with increasing concentrations of Mg2+ ions and did not reach a plateau value even at 1 M Mg2+ ions. Furthermore, this dependence on Mg2+ ions was observed in the presence of a high concentration of Li+ ions. These results indicate that the Mg2+ ion is a very effective cofactor but that the affinity of the ribozyme for a specific Mg2+ ion is very low. Moreover, cleavage by the ribozyme in the presence of both Li+ and Mg2+ ions was more effective than expected, suggesting the existence of a new reaction pathway-a cooperative pathway-in the presence of these multiple ions, and the possibility that a Mg2+ ion with weak affinity for the ribozyme is likely to function in structural support and/or act as a catalyst.
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Registered trials
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