Evidence map›Paper›PMID 23542008›Full record

ArticleJournal of molecular biology2013

Steric complementarity in the decoding center is important for tRNA selection by the ribosome.

Prashant K Khade, Xinying Shi, Simpson Joseph

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Decoding on the ribosome depends on the structure of the mRNA phosphodiester backbone.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. Ribosome dynamics during decoding.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  13. The parable of the caveman and the Ferrari: protein synthesis and the RNA world.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Structural Insights into tRNA Dynamics on the Ribosome.International journal of molecular sciences · 2015
    Review
  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

3 authors at 1 institution in 1 country.

Prashant K KhadeDepartment of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0314, USA.
Xinying Shi
Simpson Joseph
University of California, San Diego · US

Funding

Molecular Role of 16S Ribosomal RNA in TranslocationR01GM065265 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JOSEPH, SIMPSON · 2002 to 2011
$2.5M
NIGMS NIH HHS GM065265NIGMS NIH HHS R01 GM065265
6 · The paper itself

Abstract

Accurate tRNA selection by the ribosome is essential for the synthesis of functional proteins. Previous structural studies indicated that the ribosome distinguishes between cognate and near-cognate tRNAs by monitoring the geometry of the codon-anticodon helix in the decoding center using the universally conserved 16S ribosomal RNA bases G530, A1492 and A1493. These bases form hydrogen bonds with the 2'-hydroxyl groups of the codon-anticodon helix, which are expected to be disrupted with a near-cognate codon-anticodon helix. However, a recent structural study showed that G530, A1492 and A1493 form hydrogen bonds in a manner identical with that of both cognate and near-cognate codon-anticodon helices. To understand how the ribosome discriminates between cognate and near-cognate tRNAs, we made 2'-deoxynucleotide and 2'-fluoro substituted mRNAs, which disrupt the hydrogen bonds between the A site codon and G530, A1492 and A1493. Our results show that multiple 2'-deoxynucleotide substitutions in the mRNA substantially inhibit tRNA selection, whereas multiple 2'-fluoro substitutions in the mRNA have only modest effects on tRNA selection. Furthermore, the miscoding antibiotics paromomycin and streptomycin rescue the defects in tRNA selection with the multiple 2'-deoxynucleotide substituted mRNA. These results suggest that steric complementarity in the decoding center is more important than the hydrogen bonds between the A site codon and G530, A1492 and A1493 for tRNA selection.

Indexed as

AnticodonCodonEscherichia coliGuanosine TriphosphateHydrolysisNucleic Acid ConformationParomomycinPeptide Elongation Factor TuProtein BindingProtein BiosynthesisRibosomesRNA, MessengerRNA, TransferStreptomycinAnticodonCodonGuanosine TriphosphateParomomycinPeptide Elongation Factor TuRNA, MessengerRNA, TransferStreptomycinEF-Tuelongation factor TuGTP hydrolysiskineticspeptide bondprotein synthesisribosomal RNArRNA

Identifiers

PMID23542008
PMCPMC3744617
OpenAlexW2092721491

What OpenQuestion holds

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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.