ArticleRNA biology2018
Cold adaptation of tRNA nucleotidyltransferases: A tradeoff in activity, stability and fidelity.
Article in RNA biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Molecular Biology Applications of Psychrophilic Enzymes: Adaptations, Advantages, Expression, and Prospective.Applied biochemistry and biotechnology · 2024Review
- A laboratory ice machine as a cold oligotrophic artificial microbial niche for biodiscovery.Scientific reports · 2023Article
- Identification and genome-wide analysis provide insights into the genetic diversity and biotechnological potentials of novel cold-adapted Acinetobacter strain.Extremophiles : life under extreme conditions · 2023Article
- 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
- Psychrophilic Bacterial Phosphate-Biofertilizers: A Novel Extremophile for Sustainable Crop Production under Cold Environment.Microorganisms · 2021Review
- Complete Genome Sequence Analysis of Acidithiobacillus ferrivorans XJFY6S-08 Reveals Environmental Adaptation to Alpine Acid Mine Drainage.Current microbiology · 2021Article
- 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
- LOTTE-seq (Long hairpin oligonucleotide based tRNA high-throughput sequencing): specific selection of tRNAs with 3'-CCA end for high-throughput sequencing.RNA biology · 2020Article
- Article
- A Temporal Order in 5'- and 3'- Processing of Eukaryotic tRNAInternational journal of molecular sciences · 2019Article
- An improved estimation of tRNA expression to better elucidate the coevolution between tRNA abundance and codon usage in bacteria.Scientific reports · 2019Article
- A Glacier Bacterium Produces High Yield of Cryoprotective Exopolysaccharide.Frontiers in microbiology · 2019Article
- Combining crystallogenesis methods to produce diffraction-quality crystals of a psychrophilic tRNA-maturation enzyme.Acta crystallographica. Section F, Structural biology communications · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cold adaptation is an evolutionary process that has dramatic impact on enzymatic activity. Increased flexibility of the protein structure represents the main evolutionary strategy for efficient catalysis and reaction rates in the cold, but is achieved at the expense of structural stability. This results in a significant activity-stability tradeoff, as it was observed for several metabolic enzymes. In polymerases, however, not only reaction rates, but also fidelity plays an important role, as these enzymes have to synthesize copies of DNA and RNA as exact as possible. Here, we investigate the effects of cold adaptation on the highly accurate CCA-adding enzyme, an RNA polymerase that uses an internal amino acid motif within the flexible catalytic core as a template to synthesize the CCA triplet at tRNA 3'-ends. As the relative orientation of these residues determines nucleotide selection, we characterized how cold adaptation impacts template reading and fidelity. In a comparative analysis of closely related psychro-, meso-, and thermophilic enzymes, the cold-adapted polymerase shows a remarkable error rate during CCA synthesis in vitro as well as in vivo. Accordingly, CCA-adding activity at low temperatures is not only achieved at the expense of structural stability, but also results in a reduced polymerization fidelity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.