Evidence map›Paper›PMID 22505715›Full record

ArticleThe Journal of biological chemistry2012

Riboswitch (T-box)-mediated control of tRNA-dependent amidation in Clostridium acetobutylicum rationalizes gene and pathway redundancy for asparagine and asparaginyl-trnaasn synthesis.

Nizar Y Saad, Bettina Schiel, Mélanie Brayé, John T Heap, Nigel P Minton, Peter Dürre, Hubert Dominique Becker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Gene essentiality in the solventogenicApplied and environmental microbiology · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Two-codon T-box riboswitch binding two tRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. 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

7 authors at 6 institutions in 3 countries.

Nizar Y SaadUnité Mixte de Recherche "Génétique Moléculaire, Génomique, Microbiologie," CNRS, Université de Strasbourg, 21 rue René Descartes, 67084 Strasbourg, France.
Bettina Schiel
Mélanie Brayé
John T Heap
Nigel P Minton
Peter Dürre
Hubert Dominique Becker
Universität Ulm · DEGénétique Moléculaire Génomique Microbiologie · FRInstitut de Biologie Moléculaire et Cellulaire · FRNational Institute for Health Research · GBUniversité de Strasbourg · FRUniversity of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F003390/1
6 · The paper itself

Abstract

Analysis of the Gram-positive Clostridium acetobutylicum genome reveals an inexplicable level of redundancy for the genes putatively involved in asparagine (Asn) and Asn-tRNA(Asn) synthesis. Besides a duplicated set of gatCAB tRNA-dependent amidotransferase genes, there is a triplication of aspartyl-tRNA synthetase genes and a duplication of asparagine synthetase B genes. This genomic landscape leads to the suspicion of the incoherent simultaneous use of the direct and indirect pathways of Asn and Asn-tRNA(Asn) formation. Through a combination of biochemical and genetic approaches, we show that C. acetobutylicum forms Asn and Asn-tRNA(Asn) by tRNA-dependent amidation. We demonstrate that an entire transamidation pathway composed of aspartyl-tRNA synthetase and one set of GatCAB genes is organized as an operon under the control of a tRNA(Asn)-dependent T-box riboswitch. Finally, our results suggest that this exceptional gene redundancy might be interconnected to control tRNA-dependent Asn synthesis, which in turn might be involved in controlling the metabolic switch from acidogenesis to solventogenesis in C. acetobutylicum.

Indexed as

AsparagineAspartate-Ammonia LigaseBacterial ProteinsClostridium acetobutylicumRiboswitchRNA, BacterialRNA, Transfer, Amino AcylAsparagineAspartate-Ammonia LigaseBacterial ProteinsRiboswitchRNA, BacterialRNA, Transfer, Amino Acyl

Identifiers

PMID22505715
PMCPMC3370219
OpenAlexW2047620528

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.