Evidence map›Paper›PMID 9829937›Full record

ArticleJournal of bacteriology1998

The Bacillus subtilis nucleotidyltransferase is a tRNA CCA-adding enzyme.

L C Raynal, H M Krisch, A J Carpousis

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

21 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Acquisition ofMicrobial genomics · 2021
    Article
  3. Analysis of tRNAF1000Research · 2020
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Evolution of tRNA nucleotidyltransferases: a small deletion generated CC-adding enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. RNA processing and degradation in Bacillus subtilis.Microbiology and molecular biology reviews : MMBR · 2003
    Review
  18. Article
  19. 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 1 country.

L C RaynalLaboratoire de Microbiologie et Génétique Moléculaire, Centre National de la Recherche Scientifique (CNRS), Toulouse, France.
H M Krisch
A J Carpousis
Centre National de la Recherche Scientifique · FRLaboratoire de Microbiologie et Génétique Moléculaires · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There has been increased interest in bacterial polyadenylation with the recent demonstration that 3' poly(A) tails are involved in RNA degradation. Poly(A) polymerase I (PAP I) of Escherichia coli is a member of the nucleotidyltransferase (Ntr) family that includes the functionally related tRNA CCA-adding enzymes. Thirty members of the Ntr family were detected in a search of the current database of eubacterial genomic sequences. Gram-negative organisms from the beta and gamma subdivisions of the purple bacteria have two genes encoding putative Ntr proteins, and it was possible to predict their activities as either PAP or CCA adding by sequence comparisons with the E. coli homologues. Prediction of the functions of proteins encoded by the genes from more distantly related bacteria was not reliable. The Bacillus subtilis papS gene encodes a protein that was predicted to have PAP activity. We have overexpressed and characterized this protein, demonstrating that it is a tRNA nucleotidyltransferase. We suggest that the papS gene should be renamed cca, following the notation for its E. coli counterpart. The available evidence indicates that cca is the only gene encoding an Ntr protein, despite previous suggestions that B. subtilis has a PAP similar to E. coli PAP I. Thus, the activity involved in RNA 3' polyadenylation in the gram-positive bacteria apparently resides in an enzyme distinct from its counterpart in gram-negative bacteria.

Indexed as

Escherichia coli ProteinsAmino Acid SequenceBacillus subtilisBase SequenceDNA PrimersGenes, BacterialMolecular Sequence DataPhylogenyPolynucleotide AdenylyltransferaseRNA, BacterialRNA NucleotidyltransferasesRNA, TransferSequence Homology, Amino AcidDNA PrimersEscherichia coli ProteinspcnB protein, E coliPolynucleotide AdenylyltransferaseRNA, BacterialRNA NucleotidyltransferasesRNA, TransfertRNA nucleotidyltransferase

Identifiers

PMID9829937
PMCPMC107713
OpenAlexW1706771868

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.