Evidence map›Paper›PMID 22308033›Full record

ArticleThe Journal of biological chemistry2012

Structural dynamics of bacterial translation initiation factor IF2.

Hans Wienk, Evgeny Tishchenko, Riccardo Belardinelli, Simona Tomaselli, Ramachandra Dongre, Roberto Spurio, Gert E Folkers, Claudio O Gualerzi, Rolf Boelens

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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. The alarmones (p)ppGpp directly regulate translation initiation during entry into quiescence.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms.Acta crystallographica. Section D, Biological crystallography · 2013
    Article
  16. Article
  17. 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

9 authors at 2 institutions in 2 countries.

Hans WienkBijvoet Center for Biomolecular Research, NMR Spectroscopy, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Evgeny Tishchenko
Riccardo Belardinelli
Simona Tomaselli
Ramachandra Dongre
Roberto Spurio
Gert E Folkers
Claudio O Gualerzi
Rolf Boelens
Utrecht University · NLUniversità di Camerino · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial translation initiation factor IF2 promotes ribosomal subunit association, recruitment, and binding of fMet-tRNA to the ribosomal P-site and initiation dipeptide formation. Here, we present the solution structures of GDP-bound and apo-IF2-G2 of Bacillus stearothermophilus and provide evidence that this isolated domain binds the 50 S ribosomal subunit and hydrolyzes GTP. Differences between the free and GDP-bound structures of IF2-G2 suggest that domain reorganization within the G2-G3-C1 regions underlies the different structural requirements of IF2 during the initiation process. However, these structural signals are unlikely forwarded from IF2-G2 to the C-terminal fMet-tRNA binding domain (IF2-C2) because the connected IF2-C1 and IF2-C2 modules show completely independent mobility, indicating that the bacterial interdomain connector lacks the rigidity that was found in the archaeal IF2 homolog aIF5B.

Indexed as

Geobacillus stearothermophilusAmino Acid SequenceBacterial ProteinsGuanosine DiphosphateGuanosine TriphosphateModels, MolecularMolecular Sequence DataProkaryotic Initiation Factor-2Protein Structure, TertiarySequence Homology, Amino AcidBacterial ProteinsGDPNP compoundGuanosine DiphosphateGuanosine TriphosphateProkaryotic Initiation Factor-2

Identifiers

PMID22308033
PMCPMC3322840
OpenAlexW1966715771

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.