ArticleNucleic acids research2015
The identity of the discriminator base has an impact on CCA addition.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- When Paul Berg meets Donald Crothers: an achiral connection through protein biosynthesis.Nucleic acids research · 2024Article
- Substrate Affinity Versus Catalytic Efficiency: Ancestral Sequence Reconstruction of tRNA Nucleotidyltransferases Solves an Enzyme Puzzle.Molecular biology and evolution · 2022Article
- Synthetic riboswitches for the analysis of tRNA processing by eukaryotic RNase P enzymes.RNA (New York, N.Y.) · 2022Article
- Human Mitochondrial RNA Processing and Modifications: Overview.International journal of molecular sciences · 2021Review
- Adaptation of theInternational journal of molecular sciences · 2020Article
- Quantitative tRNA-sequencing uncovers metazoan tissue-specific tRNA regulation.Nature communications · 2020Article
- Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020Article
- Deep sequencing of tRNA's 3'-termini sheds light on CCA-tail integrity and maturation.RNA (New York, N.Y.) · 2020Article
- Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes.International journal of molecular sciences · 2020Article
- Exploration of CCA-added RNAs revealed the expression of mitochondrial non-coding RNAs regulated by CCA-adding enzyme.RNA biology · 2019Article
- A Temporal Order in 5'- and 3'- Processing of Eukaryotic tRNAInternational journal of molecular sciences · 2019Article
- Article
- Drugging tRNA aminoacylation.RNA biology · 2018Review
- tRNA Modifications: Impact on Structure and Thermal Adaptation.Biomolecules · 2017Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CCA-adding enzymes synthesize and maintain the C-C-A sequence at the tRNA 3'-end, generating the attachment site for amino acids. While tRNAs are the most prominent substrates for this polymerase, CCA additions on non-tRNA transcripts are described as well. To identify general features for substrate requirement, a pool of randomized transcripts was incubated with the human CCA-adding enzyme. Most of the RNAs accepted for CCA addition carry an acceptor stem-like terminal structure, consistent with tRNA as the main substrate group for this enzyme. While these RNAs show no sequence conservation, the position upstream of the CCA end was in most cases represented by an adenosine residue. In tRNA, this position is described as discriminator base, an important identity element for correct aminoacylation. Mutational analysis of the impact of the discriminator identity on CCA addition revealed that purine bases (with a preference for adenosine) are strongly favoured over pyrimidines. Furthermore, depending on the tRNA context, a cytosine discriminator can cause a dramatic number of misincorporations during CCA addition. The data correlate with a high frequency of adenosine residues at the discriminator position observed in vivo. Originally identified as a prominent identity element for aminoacylation, this position represents a likewise important element for efficient and accurate CCA addition.
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