Evidence map›Paper›PMID 16314511›Full record

ArticleMolecular and cellular biology2005

Identification of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis.

Arturas Meskauskas, Alexey N Petrov, Jonathan D Dinman

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

41 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Adaptive Response ofJournal of fungi (Basel, Switzerland) · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Ribosomal Antibiotics: Contemporary Challenges.Antibiotics (Basel, Switzerland) · 2016
    Review
  9. Article
  10. Article
  11. Bypass of the pre-60S ribosomal quality control as a pathway to oncogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Eukaryotic rpL10 drives ribosomal rotation.Nucleic acids research · 2014
    Article
  13. Article
  14. Article
  15. Review
  16. Chromatographic purification of highly active yeast ribosomes.Journal of visualized experiments : JoVE · 2011
    Article
  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

3 authors at 1 institution in 2 countries.

Arturas MeskauskasDepartment of Cell Biology and Molecular Genetics, Microbiology Building Room 2135, University of Maryland, College Park, 20742, USA.
Alexey N Petrov
Jonathan D Dinman
Laboratory of Molecular Genetics · PL

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
NIGMS NIH HHS GM58859NIGMS NIH HHS R01 GM058859
6 · The paper itself

Abstract

There is accumulating evidence that many ribosomal proteins are involved in shaping rRNA into their functionally correct conformations through RNA-protein interactions. Moreover, although rRNA seems to play the central role in all aspects of ribosome function, ribosomal proteins may be involved in facilitating communication between different functional regions in ribosome, as well as between the ribosome and cellular factors. In an effort to more fully understand how ribosomal proteins may influence ribosome function, we undertook large-scale mutational analysis of ribosomal protein L3, a core protein of the large subunit that has been implicated in numerous ribosome-associated functions in the past. A total of 98 different rpl3 alleles were genetically characterized with regard to their effects on killer virus maintenance, programmed -1 ribosomal frameshifting, resistance/hypersensitivity to the translational inhibitor anisomycin and, in specific cases, the ability to enhance translation of a reporter mRNA lacking the 5' (7)mGppp cap structure and 3' poly(A) tail. Biochemical studies reveal a correlation between an increased affinity for aminoacyl-tRNA and the extent of anisomycin resistance and a decreased peptidyltransferase activity and increased frameshifting efficiency. Immunoblot analyses reveal that the superkiller phenotype is not due to a defect in the ability of ribosomes to recruit the Ski-complex, suggesting that the defect lies in a reduced ability of mutant ribosomes to distinguish between cap(+)/poly(A)(+) and cap(-)/poly(A)(-) mRNAs. The results of these analyses are discussed with regard to how protein-rRNA interactions may affect ribosome function.

Indexed as

AllelesAmino Acid SequenceAmino Acid SubstitutionAnisomycinDrug Resistance, FungalFrameshifting, RibosomalMutagenesisMutationProtein ConformationRibosomal Protein L3Ribosomal ProteinsRibosomesRNA CapsRNA, MessengerRNA, RibosomalRNA, Transfer, Amino AcylAnisomycinRibosomal Protein L3Ribosomal ProteinsRNA CapsRNA, MessengerRNA, RibosomalRNA, Transfer, Amino AcylSaccharomyces cerevisiae Proteins

Identifiers

PMID16314511
PMCPMC1316954
OpenAlexW2168677293

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.