Evidence map›Paper›PMID 17245450›Full record

ArticlePloS one2007

Optimization of ribosome structure and function by rRNA base modification.

Jennifer L Baxter-Roshek, Alexey N Petrov, Jonathan D Dinman

Abstract read
In one paragraph

Article in PloS one, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing 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

96 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. METTL5-mediated 18S rRNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Molecular Basis of the Slow Growth ofFrontiers in cellular and infection microbiology · 2022
    Article
  18. Review
  19. Review
  20. Review

36 more citing papers are in PubMed but not listed here.

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.

Jennifer L Baxter-RoshekDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland, United States of America.
Alexey N Petrov
Jonathan D Dinman

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
Mechanisms of Virus Replication and Gene ExpressionT32AI051967 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI SIMON, ANNE ELIZABETH · 2002 to 2013
$1.8M
NIAID NIH HHS T32 AI051967NIGMS NIH HHS R01 GM058859NIGMS NIH HHS R01 GM58859
6 · The paper itself

Abstract

backgroundTranslating mRNA sequences into functional proteins is a fundamental process necessary for the viability of organisms throughout all kingdoms of life. The ribosome carries out this process with a delicate balance between speed and accuracy. This work investigates how ribosome structure and function are affected by rRNA base modification. The prevailing view is that rRNA base modifications serve to fine tune ribosome structure and function. METHODOLOGY/PRINCIPAL

findingsTo test this hypothesis, yeast strains deficient in rRNA modifications in the ribosomal peptidyltransferase center were monitored for changes in and translational fidelity. These studies revealed allele-specific sensitivity to translational inhibitors, changes in reading frame maintenance, nonsense suppression and aa-tRNA selection. Ribosomes isolated from two mutants with the most pronounced phenotypic changes had increased affinities for aa-tRNA, and surprisingly, increased rates of peptidyltransfer as monitored by the puromycin assay. rRNA chemical analyses of one of these mutants identified structural changes in five specific bases associated with the ribosomal A-site. CONCLUSIONS/SIGNIFICANCE: Together, the data suggest that modification of these bases fine tune the structure of the A-site region of the large subunit so as to assure correct positioning of critical rRNA bases involved in aa-tRNA accommodation into the PTC, of the eEF-1A.aa-tRNA.GTP ternary complex with the GTPase associated center, and of the aa-tRNA in the A-site. These findings represent a direct demonstration in support of the prevailing hypothesis that rRNA modifications serve to optimize rRNA structure for production of accurate and efficient ribosomes.

Indexed as

Nucleic Acid ConformationRNA, RibosomalAllelesBase SequenceHumansModels, MolecularMolecular Sequence DataMutationPeptidyl TransferasesProtein BiosynthesisProtein ConformationRibosomesRibosome Subunits, Large, EukaryoticRNA, Transfer, Amino Acid-SpecificPeptidyl TransferasesRNA, RibosomalRNA, Transfer, Amino Acid-Specific

Identifiers

PMID17245450
PMCPMC1766470

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.