Evidence map›Paper›PMID 19745807›Full record

ArticleThe EMBO journal2009

Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme.

Yukimatsu Toh, Daijiro Takeshita, Tomoyuki Numata, Shuya Fukai, Osamu Nureki, Kozo Tomita

Abstract read
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Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Two complementingRNA biology · 2025
    Article
  4. Crystal structure of the CCA-adding enzyme fromJournal of structural biology: X · 2025
    Article
  5. Article
  6. Article
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  8. Article
  9. Article
  10. Article
  11. Acquisition ofMicrobial genomics · 2021
    Article
  12. Article
  13. Adaptation of theInternational journal of molecular sciences · 2020
    Article
  14. Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020
    Article
  15. Article
  16. Article
  17. Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes.International journal of molecular sciences · 2020
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

6 authors.

Yukimatsu TohInstitute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Higashi, Tsukuba-shi, Ibaraki, Japan.
Daijiro Takeshita
Tomoyuki Numata
Shuya Fukai
Osamu Nureki
Kozo Tomita

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The CCA-adding enzyme synthesizes the CCA sequence at the 3' end of tRNA without a nucleic acid template. The crystal structures of class II Thermotoga maritima CCA-adding enzyme and its complexes with CTP or ATP were determined. The structure-based replacement of both the catalytic heads and nucleobase-interacting neck domains of the phylogenetically closely related Aquifex aeolicus A-adding enzyme by the corresponding domains of the T. maritima CCA-adding enzyme allowed the A-adding enzyme to add CCA in vivo and in vitro. However, the replacement of only the catalytic head domain did not allow the A-adding enzyme to add CCA, and the enzyme exhibited (A, C)-adding activity. We identified the region in the neck domain that prevents (A, C)-adding activity and defines the number of nucleotide incorporations and the specificity for correct CCA addition. We also identified the region in the head domain that defines the terminal A addition after CC addition. The results collectively suggest that, in the class II CCA-adding enzyme, the head and neck domains collaboratively and dynamically define the number of nucleotide additions and the specificity of nucleotide selection.

Indexed as

Adenosine TriphosphateAmino Acid SequenceBacteriaCatalytic DomainCrystallography, X-RayCytidine TriphosphateModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationRecombinant Fusion ProteinsRNA NucleotidyltransferasesThermotoga maritimaA adding enzymeAdenosine TriphosphateCytidine TriphosphateRecombinant Fusion ProteinsRNA NucleotidyltransferasestRNA nucleotidyltransferase

Identifiers

PMID19745807
PMCPMC2776095

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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.