ArticleProceedings of the National Academy of Sciences of the United States of America2011
An inhibitory C-terminal region dictates the specificity of A-adding enzymes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. 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, 23 citations in OpenAlex.
- Enzyme structure and kinetics produce tRNA and nucleotide specificity of Schizosaccharomyces pombe CC- and A-adding enzymes.Nucleic acids research · 2026Article
- Substrate Affinity Versus Catalytic Efficiency: Ancestral Sequence Reconstruction of tRNA Nucleotidyltransferases Solves an Enzyme Puzzle.Molecular biology and evolution · 2022Article
- CCA-Addition Gone Wild: Unusual Occurrence and Phylogeny of Four Different tRNA Nucleotidyltransferases in Acanthamoeba castellanii.Molecular biology and evolution · 2021Article
- Adaptation of theInternational journal of molecular sciences · 2020Article
- Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020Article
- Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes.International journal of molecular sciences · 2020Article
- Phylogeny and Evolution of RNA 3'-Nucleotidyltransferases in Bacteria.Journal of molecular evolution · 2019Article
- Dual expression of CCA-adding enzyme and RNase T in Escherichia coli generates a distinct cca growth phenotype with diverse applications.Nucleic acids research · 2019Article
- Cold adaptation of tRNA nucleotidyltransferases: A tradeoff in activity, stability and fidelity.RNA biology · 2018Article
- Genotyping bacterial and fungal pathogens using sequence variation in the gene for the CCA-adding enzyme.BMC microbiology · 2016Article
- The ancestor of modern Holozoa acquired the CCA-adding enzyme from Alphaproteobacteria by horizontal gene transfer.Nucleic acids research · 2015Article
- The identity of the discriminator base has an impact on CCA addition.Nucleic acids research · 2015Article
- Domain movements during CCA-addition: a new function for motif C in the catalytic core of the human tRNA nucleotidyltransferases.RNA biology · 2015Article
- Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases.Frontiers in genetics · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For efficient aminoacylation, tRNAs carry the conserved 3'-terminal sequence C-C-A, which is synthesized by highly specific tRNA nucleotidyltransferases (CCA-adding enzymes). In several prokaryotes, this function is accomplished by separate enzymes for CC- and A-addition. As A-adding enzymes carry an N-terminal catalytic core identical to that of CCA-adding enzymes, it is unclear why their activity is restricted. Here, it is shown that C-terminal deletion variants of A-adding enzymes acquire full and precise CCA-incorporating activity. The deleted region seems to be responsible for tRNA primer selection, restricting the enzyme's specificity to tRNAs ending with CC. The data suggest that A-adding enzymes carry an intrinsic CCA-adding activity that can be reactivated by the introduction of deletions in the C-terminal domain. Furthermore, a unique subtype of CCA-adding enzymes could be identified that evolved out of A-adding enzymes, suggesting that mutations and deletions in nucleotidyltransferases can lead to altered and even more complex activities, as a simple A-incorporation is converted into sequence-specific addition of C and A residues. Such activity-modifying events may have had an important role in the evolution of tRNA nucleotidyltransferases.
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