Evidence map›Paper›PMID 27986852›Full record

ArticleNucleic acids research2017

Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways.

Jorge P López-Alonso, Attilio Fabbretti, Tatsuya Kaminishi, Idoia Iturrioz, Letizia Brandi, David Gil-Carton, Claudio O Gualerzi, Paola Fucini, Sean R Connell

Abstract read
In one paragraph

Article in Nucleic acids research, 2017. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Natural Products That Contain Higher Homologated Amino Acids.Chembiochem : a European journal of chemical biology · 2024
    Review
  4. Article
  5. Total Synthesis of GE81112A: An Orthoester-Based Approach.The Journal of organic chemistry · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Hijacking Translation Initiation for Synthetic Biology.Chembiochem : a European journal of chemical biology · 2020
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Ribosome Structure, Function, and Early Evolution.International journal of molecular sciences · 2018
    Review
  17. Complementary charge-based interaction between the ribosomal-stalk protein L7/12 and IF2 is the key to rapid subunit association.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Review
  19. 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.

Jorge P López-AlonsoStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
Attilio FabbrettiLaboratory of Genetics, University of Camerino, 62032 Camerino, Italy.
Tatsuya KaminishiStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
Idoia IturriozStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
Letizia BrandiLaboratory of Genetics, University of Camerino, 62032 Camerino, Italy.
David Gil-CartonStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
Claudio O GualerziLaboratory of Genetics, University of Camerino, 62032 Camerino, Italy.
Paola FuciniStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.
Sean R ConnellStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In bacteria, the start site and the reading frame of the messenger RNA are selected by the small ribosomal subunit (30S) when the start codon, typically an AUG, is decoded in the P-site by the initiator tRNA in a process guided and controlled by three initiation factors. This process can be efficiently inhibited by GE81112, a natural tetrapeptide antibiotic that is highly specific toward bacteria. Here GE81112 was used to stabilize the 30S pre-initiation complex and obtain its structure by cryo-electron microscopy. The results obtained reveal the occurrence of changes in both the ribosome conformation and initiator tRNA position that may play a critical role in controlling translational fidelity. Furthermore, the structure highlights similarities with the early steps of initiation in eukaryotes suggesting that shared structural features guide initiation in all kingdoms of life.

Indexed as

Peptide Chain Initiation, TranslationalBinding SitesEscherichia coliEukaryotic CellsModels, MolecularMolecular ConformationProkaryotic Initiation FactorsProtein BiosynthesisRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialRNA, MessengerRNA, Transfer, MetProkaryotic Initiation FactorsRNA, MessengerRNA, Transfer, Met

Identifiers

PMID27986852
PMCPMC5389724

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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.