Evidence map›Paper›PMID 7623843›Full record

ArticleMolecular and cellular biology1995

Mutational analysis of the Prt1 protein subunit of yeast translation initiation factor 3.

D R Evans, C Rasmussen, P J Hanic-Joyce, G C Johnston, R A Singer, C A Barnes

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

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0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

17 citing papers in PubMed.

  1. The Biological Roles of Translation Initiation Factor 3b.International journal of biological sciences · 2018
    Review
  2. Article
  3. Molecular mechanism of scanning and start codon selection in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2011
    Review
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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

6 authors.

D R EvansDepartment of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.
C Rasmussen
P J Hanic-Joyce
G C Johnston
R A Singer
C A Barnes

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Saccharomyces cerevisiae PRT1 gene product Prt1p is a component of translation initiation factor eIF-3, and mutations in PRT1 inhibit translation initiation. We have investigated structural and functional aspects of Prt1p and its gene. Transcript analysis and deletion of the PRT1 5' end revealed that translation of PRT1 mRNA is probably initiated at the second in-frame ATG in the open reading frame. The amino acid changes encoded by six independent temperature-sensitive prt1 mutant alleles were found to be distributed throughout the central and C-terminal regions of Prt1p. The temperature sensitivity of each mutant allele was due to a single missense mutation, except for the prt1-2 allele, in which two missense mutations were required. In-frame deletion of an N-terminal region of Prt1p generated a novel, dominant-negative form of Prt1p that inhibits translation initiation even in the presence of wild-type Prt1p. Subcellular fractionation suggested that the dominant-negative Prt1p competes with wild-type Prt1p for association with a component of large Prt1p complexes and as a result inhibits the binding of wild-type Prt1p to the 40S ribosome.

Indexed as

Peptide Chain Initiation, TranslationalSaccharomyces cerevisiae ProteinsAllelesAmino Acid SequenceBase SequenceCloning, MolecularDNA Mutational AnalysisEukaryotic Initiation Factor-3Fungal ProteinsMacromolecular SubstancesMolecular Sequence DataOpen Reading FramesPeptide FragmentsPeptide Initiation FactorsPolymorphism, GeneticProkaryotic Initiation Factor-3Eukaryotic Initiation Factor-3Fungal ProteinsMacromolecular SubstancesPeptide FragmentsPeptide Initiation FactorsProkaryotic Initiation Factor-3Protein Synthesis InhibitorsPrt1 protein, S cerevisiaeRNA-Binding ProteinsRNA PrecursorsSaccharomyces cerevisiae Proteins

Identifiers

PMID7623843
PMCPMC230692

What OpenQuestion holds

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Registered trials

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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.