Evidence map›Paper›PMID 20155482›Full record

ReviewCellular and molecular life sciences : CMLS2010

tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.

Heike Betat, Christiane Rammelt, Mario Mörl

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Two complementingRNA biology · 2025
    Article
  3. Crystal structure of the CCA-adding enzyme fromJournal of structural biology: X · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Adaptation of theInternational journal of molecular sciences · 2020
    Article
  11. Origin and Evolution ofMicroorganisms · 2020
    Article
  12. Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020
    Article
  13. Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes.International journal of molecular sciences · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. A Temporal Order in 5'- and 3'- Processing of Eukaryotic tRNAInternational journal of molecular sciences · 2019
    Article
  19. Transcriptome and Proteome Response ofFrontiers in physiology · 2019
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Heike BetatInstitute for Biochemistry, University of Leipzig, Brüderstr. 34, 04103 Leipzig, Germany.
Christiane Rammelt
Mario Mörl
Leipzig University · DELuther University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA polymerases are important enzymes involved in the realization of the genetic information encoded in the genome. Thereby, DNA sequences are used as templates to synthesize all types of RNA. Besides these classical polymerases, there exists another group of RNA polymerizing enzymes that do not depend on nucleic acid templates. Among those, tRNA nucleotidyltransferases show remarkable and unique features. These enzymes add the nucleotide triplet C-C-A to the 3'-end of tRNAs at an astonishing fidelity and are described as "CCA-adding enzymes". During this incorporation of exactly three nucleotides, the enzymes have to switch from CTP to ATP specificity. How these tasks are fulfilled by rather simple and small enzymes without the help of a nucleic acid template is a fascinating research area. Surprising results of biochemical and structural studies allow scientists to understand at least some of the mechanistic principles of the unique polymerization mode of these highly unusual enzymes.

Indexed as

Amino Acid SequenceBase SequenceBinding SitesDNA-Directed RNA PolymerasesEvolution, MolecularModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProtein ConformationRNA NucleotidyltransferasesRNA, TransferTelomeraseDNA-Directed RNA PolymerasesRNA NucleotidyltransferasesRNA, TransferTelomerasetRNA nucleotidyltransferase

Identifiers

PMID20155482
PMCPMC11115931
OpenAlexW2017821098

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.