ArticleNucleic acids research2002
Outersphere and innersphere coordinated metal ions in an aminoacyl-tRNA synthetase ribozyme.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 30 citations in OpenAlex.
- Variation in phylogenetic tendencies of contiguous riboswitches.Microbial genomics · 2025Article
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- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Magnesium Signaling in Plants.International journal of molecular sciences · 2021Review
- An aminoacylation ribozyme evolved from a natural tRNA-sensing T-box riboswitch.Nature chemical biology · 2020Article
- TbFrontiers in chemistry · 2017Article
- The RNA origin of transfer RNA aminoacylation and beyond.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Article
- Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme.Nature · 2008Article
- Characterizing riboswitch function: identification of Mg2+ binding site in T box antiterminator RNA.Biochemical and biophysical research communications · 2008Article
- Structure and binding of Mg(II) ions and di-metal bridge complexes with biological phosphates and phosphoranes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2004Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Metal ions are essential cofactors for various ribozymes. Here we dissect the roles of metal ions in an aminoacyl-tRNA synthetase-like ribozyme (ARS ribozyme), which was evolved in vitro. This ribozyme can charge phenylalanine on tRNA in cis, where it is covalently attached to the 5'-end of tRNA (i.e. a form of precursor tRNA), as well as in trans, where it can act as a catalyst. The presence of magnesium ion is essential for this ribozyme to exhibit full catalytic activity. Metal-dependent kinetics, as well as structural mappings using Tb3+ in competition with Mg2+ or Co(NH3)6(3+), identified two potential metal-binding sites which are embedded near the tRNA-binding site. The high affinity metal-binding site can be filled with either Mg2+ or Co(NH3)6(3+) and thus the activity relies on a metal ion that is fully coordinated with water or ammonium ions. This site also overlaps with the amino acid-binding site, suggesting that the metal ion plays a role in constituting the catalytic core. The weak metal-binding site is occupied only by a metal ion(s) that can form innersphere contacts with ligands in the ribozyme and, hence, Mg2+ can enhance ribozyme activity, but Co(NH3)6(3+) cannot. The experiments described in this work establish the roles of metal ions that have distinct coordination properties in the ARS ribozyme.
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