Evidence map›Paper›PMID 18682528›Full record

ArticleNucleic acids research2008

A comparative analysis of two conserved motifs in bacterial poly(A) polymerase and CCA-adding enzyme.

Andrea Just, Falk Butter, Michelle Trenkmann, Tony Heitkam, Mario Mörl, Heike Betat

Open access · goldAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Two complementingRNA biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Adaptation of theInternational journal of molecular sciences · 2020
    Article
  7. Divergent Evolution of Eukaryotic CC- and A-Adding Enzymes.International journal of molecular sciences · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. An inhibitory C-terminal region dictates the specificity of A-adding enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Review
  19. Bacterial/archaeal/organellar polyadenylation.Wiley interdisciplinary reviews. RNA
    Review
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

6 authors at 1 institution in 1 country.

Andrea JustInstitute for Biochemistry, University of Leipzig, Brüderstr. 34, 04103 Leipzig, Germany.
Falk Butter
Michelle Trenkmann
Tony Heitkam
Mario Mörl
Heike Betat
Leipzig University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Showing a high sequence similarity, the evolutionary closely related bacterial poly(A) polymerases (PAP) and CCA-adding enzymes catalyze quite different reactions--PAP adds poly(A) tails to RNA 3'-ends, while CCA-adding enzymes synthesize the sequence CCA at the 3'-terminus of tRNAs. Here, two highly conserved structural elements of the corresponding Escherichia coli enzymes were characterized. The first element is a set of amino acids that was identified in CCA-adding enzymes as a template region determining the enzymes' specificity for CTP and ATP. The same element is also present in PAP, where it confers ATP specificity. The second investigated region corresponds to a flexible loop in CCA-adding enzymes and is involved in the incorporation of the terminal A-residue. Although, PAP seems to carry a similar flexible region, the functional relevance of this element in PAP is not known. The presented results show that the template region has an essential function in both enzymes, while the second element is surprisingly dispensable in PAP. The data support the idea that the bacterial PAP descends from CCA-adding enzymes and still carries some of the structural elements required for CCA-addition as an evolutionary relic and is now fixed in a conformation specific for A-addition.

Indexed as

Amino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionConserved SequenceEscherichia coliEscherichia coli ProteinsMolecular Sequence DataNucleotidesPolyadenylationPolynucleotide AdenylyltransferaseRNA NucleotidyltransferasesSequence Homology, Amino AcidSubstrate SpecificityEscherichia coli ProteinsNucleotidesPolynucleotide AdenylyltransferaseRNA NucleotidyltransferasestRNA nucleotidyltransferase

Identifiers

PMID18682528
PMCPMC2532741
OpenAlexW2161671944

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.