Evidence map›Paper›PMID 16166657›Full record

ArticleNucleic acids research2005

Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu.

George Dinos, Dimitrios L Kalpaxis, Daniel N Wilson, Knud H Nierhaus

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2005. 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
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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  7. Article
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  9. Model of the pathway of -1 frameshifting: Kinetics.Biochemistry and biophysics reports · 2016
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Navigating the ribosome's metastable energy landscape.Trends in biochemical sciences · 2009
    Review
  16. Review
  17. Shine-Dalgarno interaction prevents incorporation of noncognate amino acids at the codon following the AUG.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  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

4 authors at 1 institution in 1 country.

George DinosMax-Planck-Institut für Molekulare Genetik AG Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany.
Dimitrios L Kalpaxis
Daniel N Wilson
Knud H Nierhaus
Max Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The presence or absence of deacylated tRNA at the E site sharply influences the activation energy required for binding of a ternary complex to the ribosomal A site indicating the different conformations that the E-tRNA imparts on the ribosome. Here we address two questions: (i) whether or not peptidyltransferase--the essential catalytic activity of the large ribosomal subunit--also depends on the occupancy state of the E site and (ii) at what stage the E-tRNA is released during an elongation cycle. Kinetics of the puromycin reaction on various functional states of the ribosome indicate that the A-site substrate of the peptidyltransferase center, puromycin, requires the same activation energy for peptide-bond formation under all conditions tested. We further demonstrate that deacylated tRNA is released from the E site by binding a ternary complex aminoacyl-tRNA*EF-Tu*GDPNP to the A site. This observation indicates that the E-tRNA is released after the decoding step but before both GTP hydrolysis by EF-Tu and accommodation of the A-tRNA. Collectively these results reveal that the reciprocal linkage between the E and A sites affects the decoding center on the 30S subunit, but does not influence the rate of peptide-bond formation at the active center of the 50S subunit.

Indexed as

Peptide Chain Elongation, TranslationalGuanosine TriphosphateKineticsModels, GeneticPeptide Elongation Factor TuPeptidyl TransferasesPuromycinRibosomesRNA, TransferTransfer RNA AminoacylationGuanosine TriphosphatePeptide Elongation Factor TuPeptidyl TransferasesPuromycinRNA, Transfer

Identifiers

PMID16166657
PMCPMC1216338
OpenAlexW2062546034

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.