ArticleNucleic acids research2010
Unusual evolution of a catalytic core element in CCA-adding enzymes.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Enzyme structure and kinetics produce tRNA and nucleotide specificity of Schizosaccharomyces pombe CC- and A-adding enzymes.Nucleic acids research · 2026Article
- Two complementingRNA biology · 2025Article
- Depletion of tRNA CCA-adding enzyme in Mycobacterium tuberculosis leads to polyadenylation of transcripts and precursor tRNAs.Scientific reports · 2023Article
- 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
- CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacteriumComputational and structural biotechnology journal · 2021Article
- Adaptation of theInternational 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
- An inhibitory C-terminal region dictates the specificity of A-adding enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
CCA-adding enzymes are polymerases existing in two distinct enzyme classes that both synthesize the C-C-A triplet at tRNA 3'-ends. Class II enzymes (found in bacteria and eukaryotes) carry a flexible loop in their catalytic core required for switching the specificity of the nucleotide binding pocket from CTP- to ATP-recognition. Despite this important function, the loop sequence varies strongly between individual class II CCA-adding enzymes. To investigate whether this loop operates as a discrete functional entity or whether it depends on the sequence context of the enzyme, we introduced reciprocal loop replacements in several enzymes. Surprisingly, many of these replacements are incompatible with enzymatic activity and inhibit ATP-incorporation. A phylogenetic analysis revealed the existence of conserved loop families. Loop replacements within families did not interfere with enzymatic activity, indicating that the loop function depends on a sequence context specific for individual enzyme families. Accordingly, modeling experiments suggest specific interactions of loop positions with important elements of the protein, forming a lever-like structure. Hence, although being part of the enzyme's catalytic core, the loop region follows an extraordinary evolutionary path, independent of other highly conserved catalytic core elements, but depending on specific sequence features in the context of the individual enzymes.
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