ArticleProceedings of the National Academy of Sciences of the United States of America2007
Reengineering CCA-adding enzymes to function as (U,G)- or dCdCdA-adding enzymes or poly(C,A) and poly(U,G) polymerases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Distribution of poly(A) polymerase I in bacteria: an expanded role for horizontal gene transfer.Microbiology (Reading, England) · 2026Article
- Two complementingRNA biology · 2025Article
- Thioesters Support Efficient Protein Biosynthesis by the Ribosome.ACS central science · 2025Article
- Acquisition ofMicrobial genomics · 2021Article
- CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacteriumComputational and structural biotechnology journal · 2021Article
- 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
- The notorious R.N.A. in the spotlight - drug or target for the treatment of disease.RNA biology · 2017Review
- 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
- Role of tRNA amino acid-accepting end in aminoacylation and its quality control.Nucleic acids research · 2011Article
- tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.Cellular and molecular life sciences : CMLS · 2010Review
- A comparative analysis of two conserved motifs in bacterial poly(A) polymerase and CCA-adding enzyme.Nucleic acids research · 2008Article
- Evolution of tRNA nucleotidyltransferases: a small deletion generated CC-adding enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases.Methods (San Diego, Calif.) · 2008Article
- RNA-specific ribonucleotidyl transferases.RNA (New York, N.Y.) · 2007Review
- Controlling translation via modulation of tRNA levels.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
3 authors.
Funding
Abstract
CCA-adding enzymes build and repair the 3'-terminal CCA sequence of tRNA. These unusual RNA polymerases use either a ribonucleoprotein template (class I) or pure protein template (class II) to form mock base pairs with the Watson-Crick edges of incoming CTP and ATP. Guided by the class II Bacillus stearothermophilus CCA-adding enzyme structure, we introduced mutations designed to reverse the polarity of hydrogen bonds between the nucleobases and protein template. We were able to transform the CCA-adding enzyme into a (U,G)-adding enzyme that incorporates UTP and GTP instead of CTP and ATP; we transformed the related Aquifex aeolicus CC- and A-adding enzymes into UU- and G-adding enzymes and Escherichia coli poly(A) polymerase into a poly(G) polymerase; and we transformed the B. stearothermophilus CCA-adding enzyme into a poly(C,A) polymerase by mutations in helix J that appear, based on the apoenzyme structure, to sterically limit addition to CCA. We also transformed the B. stearothermophilus CCA-adding enzyme into a dCdCdA-adding enzyme by mutating an arginine that interacts with the incoming ribose 2' hydroxyl. Most importantly, we found that mutations in helix J can affect the specificity of the nucleotide binding site some 20 A away, suggesting that the specificity of both class I and II enzymes may be dictated by an intricate network of hydrogen bonds involving the protein, incoming nucleotide, and 3' end of the tRNA. Collaboration between RNA and protein in the form of a ribonucleoprotein template may help to explain the evolutionary diversity of the nucleotidyltransferase family.
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