Evidence map›Paper›PMID 9528754›Full record

ArticleMolecular and cellular biology1998

Functional interactions between yeast mitochondrial ribosomes and mRNA 5' untranslated leaders.

N S Green-Willms, T D Fox, M C Costanzo

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Molecular and cellular biology · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Massive programmed translational jumping in mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Chloroplast protein targeting involves localized translation in Chlamydomonas.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  11. The ribosome filter redux.Cell cycle (Georgetown, Tex.) · 2007
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

3 authors at 1 institution in 1 country.

N S Green-WillmsSection of Genetics and Development, Cornell University, Ithaca, New York 14853-2703, USA.
T D Fox
M C Costanzo
Cornell University · US

Funding

TRANSLATIONAL CONTROL OF YEAST MITOCHONDRIAL GENESR01GM029362 · NIGMS · CORNELL UNIVERSITY ITHACA · PI FOX, THOMAS DAVID · 1985 to 2013
$6.1M
PREDOCTORAL TRAINING IN GENETICS AND DEVELOPMENTT32GM007617 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BARBASH, DANIEL A · 1985 to 2021
$5.5M
NIGMS NIH HHS GM07617NIGMS NIH HHS GM29362NIGMS NIH HHS R01 GM029362NIGMS NIH HHS T32 GM007617
6 · The paper itself

Abstract

Translation of mitochondrial mRNAs in Saccharomyces cerevisiae depends on mRNA-specific translational activators that recognize the 5' untranslated leaders (5'-UTLs) of their target mRNAs. We have identified mutations in two new nuclear genes that suppress translation defects due to certain alterations in the 5'-UTLs of both the COX2 and COX3 mRNAs, indicating a general function in translational activation. One gene, MRP21, encodes a protein with a domain related to the bacterial ribosomal protein S21 and to unidentified proteins of several animals. The other gene, MRP51, encodes a novel protein whose only known homolog is encoded by an unidentified gene in S. kluyveri. Deletion of either MRP21 or MRP51 completely blocked mitochondrial gene expression. Submitochondrial fractionation showed that both Mrp21p and Mrp51p cosediment with the mitochondrial ribosomal small subunit. The suppressor mutations are missense substitutions, and those affecting Mrp21p alter the region homologous to E. coli S21, which is known to interact with mRNAs. Interactions of the suppressor mutations with leaky mitochondrial initiation codon mutations strongly suggest that the suppressors do not generally increase translational efficiency, since some alleles that strongly suppress 5'-UTL mutations fail to suppress initiation codon mutations. We propose that mitochondrial ribosomes themselves recognize a common feature of mRNA 5'-UTLs which, in conjunction with mRNA-specific translational activation, is required for organellar translation initiation.

Indexed as

Suppression, GeneticAllelesAmino Acid SequenceCloning, MolecularCyclooxygenase 2Electron Transport Complex IVIsoenzymesMembrane ProteinsMitochondriaMolecular Sequence DataPoint MutationProstaglandin-Endoperoxide SynthasesProtein BiosynthesisRibosomal ProteinsRibosomesRNA, MessengerCOX3 protein, S cerevisiaeCyclooxygenase 2Electron Transport Complex IVIsoenzymesMembrane Proteinsmitochondrial messenger RNAMRP21 protein, S cerevisiaeMRP51 protein, S cerevisiaeProstaglandin-Endoperoxide SynthasesRibosomal Proteinsribosomal protein S21RNA, MessengerRNA, MitochondrialSaccharomyces cerevisiae Proteins

Identifiers

PMID9528754
PMCPMC121412
OpenAlexW2147730875

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.