ArticleRNA (New York, N.Y.)2009
Distinct kinetic determinants for the stepwise CCA addition to tRNA.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Two complementingRNA biology · 2025Article
- Substrate Affinity Versus Catalytic Efficiency: Ancestral Sequence Reconstruction of tRNA Nucleotidyltransferases Solves an Enzyme Puzzle.Molecular biology and evolution · 2022Article
- 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
- Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020Article
- Hijacking tRNAs From Translation: Regulatory Functions of tRNAs in Mammalian Cell Physiology.Frontiers in molecular biosciences · 2020Review
- tRNA 3'-amino-tailing for stable amino acid attachment.RNA (New York, N.Y.) · 2018Article
- Cold adaptation of tRNA nucleotidyltransferases: A tradeoff in activity, stability and fidelity.RNA biology · 2018Article
- Molecular Basis and Consequences of the Cytochrome c-tRNA Interaction.The Journal of biological chemistry · 2016Article
- Domain movements during CCA-addition: a new function for motif C in the catalytic core of the human tRNA nucleotidyltransferases.RNA biology · 2015Article
- tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.Cellular and molecular life sciences : CMLS · 2010Review
- CCA addition to tRNA: implications for tRNA quality control.IUBMB life · 2010Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The universally conserved CCA sequence is present at the 3' terminal 74-76 positions of all active tRNA molecules as a functional tag to participate in ribosome protein synthesis. The CCA enzyme catalyzes CCA synthesis in three sequential steps of nucleotide addition at rapid and identical rates. However, the kinetic determinant of each addition is unknown, thus limiting the insights into the kinetic basis of CCA addition. Using our recently developed single turnover kinetics of Escherichia coli CCA enzyme as a model, we show here that the identical rate of the stepwise CCA addition is determined by distinct kinetic parameters. Specifically, the kinetics of C74 and C75 addition is controlled by the chemistry of nucleotidyl transfer, whereas the kinetics of A76 addition is controlled by a prechemistry conformational transition of the active site. In multiple turnover condition, all three steps are controlled by slow product release, indicating enzyme processivity from one addition to the next. However, the processivity decreases as the enzyme progresses to complete the CCA synthesis. Together, these results suggest the existence of a network of diverse kinetic parameters that determines the overall rate of CCA addition for tRNA maturation.
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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.