Evidence map›Paper›PMID 8167413›Full record

ArticleMolecular biology of the cell1993

Alteration of the Saccharomyces cerevisiae COX2 mRNA 5'-untranslated leader by mitochondrial gene replacement and functional interaction with the translational activator protein PET111.

J J Mulero, T D Fox

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

37 citing papers in PubMed, 73 citations in OpenAlex.

  1. Allotopic expression ofLife science alliance · 2023
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  8. Review
  9. The Cox3p assembly module of yeast cytochrome oxidase.Molecular biology of the cell · 2014
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  19. Expression of Barstar as a selectable marker in yeast mitochondria.Molecular genetics and genomics : MGG · 2003
    Article
  20. The Rieske FeS protein encoded and synthesized within mitochondria complements a deficiency in the nuclear gene.Proceedings of the National Academy of Sciences of the United States of America · 2003
    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.

J J MuleroSections of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853-2703.
T D Fox
Cornell University · US

Funding

TRANSLATIONAL CONTROL OF YEAST MITOCHONDRIAL GENESR01GM029362 · NIGMS · CORNELL UNIVERSITY ITHACA · PI FOX, THOMAS DAVID · 1985 to 2013
$6.1M
NIGMS NIH HHS GM-29362
6 · The paper itself

Abstract

The ability to replace wild-type mitochondrial DNA sequences in yeast with in vitro-generated mutations has been exploited to study the mechanism by which the nuclearly encoded PET111 protein specifically activates translation of the mitochondrially coded COX2 mRNA. We have generated three mutations in vitro that alter the COX2 mRNA 5'-untranslated leader (UTL) and introduced them into the mitochondrial genome, replacing the wild-type sequence. None of the mutations significantly affected the steady-state level of COX2 mRNA. Deletion of a single base at position -24 (relative to the translation initiation codon) in the 5'-UTL (cox2-11) reduced COX2 mRNA translation and respiratory growth, whereas insertion of four bases in place of the deleted base (cox2-12) and deletion of bases -30 to -2 (cox2-13) completely blocked both. Six spontaneous nuclear mutations were selected as suppressors of the single-base 5'-UTL deletion, cox2-11. One of these mapped to PET111 and was shown to be a missense mutation that changed residue 652 from Ala to Thr. This suppressor, PET111-20, failed to suppress the 29-base deletion, cox2-13, but very weakly suppressed the insertion mutation, cox2-12. PET111-20 also enhanced translation of a partially functional COX2 mRNA with a wild-type 5'-UTL but a mutant initiation codon. Although overexpression of the wild-type PET111 protein caused weak suppression of the single-base deletion, cox2-11, the PET111-20 suppressor mutation did not function simply by increasing the level of the protein. These results demonstrate an intimate functional interaction between the translational activator protein and the mRNA 5'-UTL and suggest that they may interact directly.

Indexed as

Protein BiosynthesisSaccharomyces cerevisiae ProteinsAllelesBase SequenceChromosomes, FungalDNA, MitochondrialElectron Transport Complex IVFungal ProteinsGenes, FungalGenetic Complementation TestMembrane ProteinsMitochondrial ProteinsMolecular Sequence DataMutagenesis, Site-DirectedNuclear ProteinsPeptide Initiation FactorsDNA, MitochondrialElectron Transport Complex IVFungal ProteinsMembrane ProteinsMitochondrial ProteinsNuclear ProteinsPeptide Initiation FactorsPET111 protein, S cerevisiaeRecombinant Fusion ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID8167413
PMCPMC275768
OpenAlexW2031809980

What OpenQuestion holds

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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.