Evidence map›Paper›PMID 22378789›Full record

ArticleThe Journal of biological chemistry2012

Further in vitro exploration fails to support the allosteric three-site model.

Alexandros D Petropoulos, Rachel Green

Abstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Ribosome collisions alter frameshifting at translational reprogramming motifs in bacterial mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Translation Elongation and Recoding in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  6. Review
  7. Three tRNAs on the ribosome slow translation elongation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Frameshifting dynamics.Biopolymers · 2013
    Review
  13. Article
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Alexandros D PetropoulosHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Rachel Green

Funding

The role played by the RNAs and tRNAs in translationR01GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1999 to 2013
$3.4M
Howard Hughes Medical InstituteNIGMS NIH HHS GM059425NIGMS NIH HHS R01 GM059425
6 · The paper itself

Abstract

Ongoing debate in the ribosome field has focused on the role of bound E-site tRNA and the Shine-Dalgarno-anti-Shine-Dalgarno (SD-aSD) interaction on A-site tRNA interactions and the fidelity of tRNA selection. Here we use an in vitro reconstituted Escherichia coli translation system to explore the reported effects of E-site-bound tRNA and SD-aSD interactions on tRNA selection events and find no evidence for allosteric coupling. A large set of experiments exploring the role of the E-site tRNA in miscoding failed to recapitulate the observations of earlier studies (Di Giacco, V., Márquez, V., Qin, Y., Pech, M., Triana-Alonso, F. J., Wilson, D. N., and Nierhaus, K. H. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 10715-10720 and Geigenmüller, U., and Nierhaus, K. H. (1990) EMBO J. 9, 4527-4533); the frequency of miscoding was unaffected by the presence of E-site-bound cognate tRNA. Moreover, our data provide clear evidence that the reported effects of the SD-aSD interaction on fidelity can be attributed to the binding of ribosomes to an unanticipated site on the mRNA (in the absence of the SD sequence) that provides a cognate pairing codon leading naturally to incorporation of the purported "noncognate" amino acid.

Indexed as

Peptide Chain Elongation, TranslationalAllosteric RegulationAllosteric SiteAmino Acid SequenceBase PairingBase SequenceChromatography, High Pressure LiquidCodonEscherichia coliPeptide Chain Initiation, TranslationalProtein BiosynthesisRibosomesRNA, BacterialRNA, MessengerRNA, Transfer, Amino AcylCodonRNA, BacterialRNA, MessengerRNA, Transfer, Amino Acyl

Identifiers

PMID22378789
PMCPMC3320913

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.