Evidence map›Paper›PMID 11497428›Full record

ArticleRNA (New York, N.Y.)2001

Ribosomal protein L5 helps anchor peptidyl-tRNA to the P-site in Saccharomyces cerevisiae.

A Meskauskas, J D Dinman

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

36 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Molecular characterization and expression analysis ofSaudi journal of biological sciences · 2021
    Article
  3. Review
  4. Article
  5. Translation Elongation and Recoding in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  6. Global shape mimicry of tRNA within a viral internal ribosome entry site mediates translational reading frame selection.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Article
  8. Review
  9. Eukaryotic rpL10 drives ribosomal rotation.Nucleic acids research · 2014
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The eukaryotic ribosome: current status and challenges.The Journal of biological chemistry · 2009
    Review
  17. 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

2 authors at 1 institution in 1 country.

A MeskauskasDepartment of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway 08854, USA.
J D Dinman
Rutgers, The State University of New Jersey · US

Funding

Translational Fidelity in EukaryotesR01GM058859 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI DINMAN, JONATHAN D · 1999 to 2011
$3.8M
RIBOSOMAL FRAMESHIFTING AS A PROBE OF 5S RRNA FUNCTIONR01GM062143 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI DINMAN, JONATHAN D. · 2001 to 2004
$726k
NIGMS NIH HHS R01 GM058859NIGMS NIH HHS R01 GM062143NIGMS NIH HHS R01 GM58859NIGMS NIH HHS R01 GM62143
6 · The paper itself

Abstract

Our previous demonstration that mutants of 5S rRNA called mof9 can specifically alter efficiencies of programmed ribosomal frameshifting (PRF) suggested a role for this ubiquitous molecule in the maintenance of translational reading frame, though the repetitive nature of the 5S rDNA gene (>100 copies/cell) inhibited more detailed analyses. However, given the known interactions between 5S rRNA and ribosomal protein L5 (previously called L1 or YL3) encoded by an essential, single-copy gene, we monitored the effects of a series of well-defined rpl5 mutants on PRF and virus propagation. Consistent with the mof9 results, we find that the rpl5 mutants promoted increased frameshifting efficiencies in both the -1 and +1 directions, and conferred defects in the ability of cells to propagate two endogenous viruses. Biochemical analyses demonstrated that mutant ribosomes had decreased affinities for peptidyl-tRNA. Pharmacological studies showed that sparsomycin, a peptidyltransferase inhibitor that specifically increases the binding of peptidyl-tRNA with ribosomes, was antagonistic to the frameshifting defects of the most severe mutant, and the extent of sparsomycin resistance correlated with the severity of the frameshifting defects in all of the mutants. These results provide biochemical and physiological evidence that one function of L5 is to anchor peptidyl-tRNA to the P-site. A model is presented describing how decreased affinity of ribosomes for peptidyl-tRNA can affect both -1 and +1 frameshifting, and for the effects of sparsomycin.

Indexed as

AllelesAnisomycinAntibiotics, AntineoplasticDose-Response Relationship, DrugFrameshift MutationMutationPeptidyl TransferasesPhenotypePlasmidsProtein BiosynthesisProtein Synthesis InhibitorsRetroelementsRibosomal ProteinsRibosomesRNA, TransferSaccharomyces cerevisiaeAnisomycinAntibiotics, AntineoplasticPeptidyl TransferasesProtein Synthesis InhibitorsRetroelementsribosomal protein L5Ribosomal ProteinsRNA, TransferSparsomycin

Identifiers

PMID11497428
PMCPMC1307509
OpenAlexW2172095534

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.