Evidence map›Paper›PMID 12637560›Full record

ArticleThe Journal of biological chemistry2003

Multiple interactions involving the amino-terminal domain of yeast mtRNA polymerase determine the efficiency of mitochondrial protein synthesis.

Matthew S Rodeheffer, Gerald S Shadel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

36 citing papers in PubMed, 70 citations in OpenAlex.

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  11. Mitochondrial ribosomal protein L12 selectively associates with human mitochondrial RNA polymerase to activate transcription.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  12. Mitochondrial DNA transcription regulation and nucleoid organization.Journal of inherited metabolic disease · 2011
    Review
  13. Mitochondrial DNA mutations in disease and aging.The Journal of cell biology · 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

2 authors at 1 institution in 1 country.

Matthew S RodehefferDepartment of Biochemistry and the Graduate Program in Biochemistry, Cell and Developmental Biology, Rollins Research Center, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA.
Gerald S Shadel
Emory University · US

Funding

Nuclear Control of Mitochondrial Gene ExpressionR01HL059655 · NHLBI · YALE UNIVERSITY · PI SHADEL, GERALD · 1997 to 2011
$3.1M
NHLBI NIH HHS HL59655NHLBI NIH HHS R01 HL059655
6 · The paper itself

Abstract

The amino-terminal domain (ATD) of Saccharomyces cerevisiae mitochondrial RNA polymerase has been shown to provide a functional link between transcription and post-transcriptional events during mitochondrial gene expression. This connection is mediated in large part by its interactions with the matrix protein Nam1p and, based on genetic phenotypes, the mitochondrial membrane protein Sls1p. These observations led us to propose previously that mtRNA polymerase, Nam1p, and Sls1p work together to coordinate transcription and translation of mtDNA-encoded gene products. Here we demonstrate by specific labeling of mitochondrial gene products in vivo that Nam1p and Sls1p indeed work together in a pathway that is required globally for efficient mitochondrial translation. Likewise, mutations in the ATD result in similar global reductions in mitochondrial translation efficiency and sensitivity to the mitochondrial translation inhibitor erythromycin. These data, coupled with the observation that the ATD is required to co-purify Sls1p in association with mtDNA nucleoids, suggest that efficient expression of mtDNA-encoded genes in yeast involves a complex series of interactions that localize active transcription complexes to the inner membrane in order to coordinate translation with transcription.

Indexed as

Fungal ProteinsSaccharomyces cerevisiae ProteinsBlotting, SouthernBlotting, WesternCarrier ProteinsCell NucleusDNA-Directed RNA PolymerasesErythromycinMembrane ProteinsMitochondriaMitochondrial ProteinsModels, BiologicalMutationPhenotypePlasmidsProtein BiosynthesisCarrier ProteinsDNA-Directed RNA PolymerasesErythromycinFungal ProteinsMembrane ProteinsMitochondrial ProteinsMTF2 protein, S cerevisiaeRNARNA, MitochondrialSaccharomyces cerevisiae ProteinsSLS1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID12637560
PMCPMC2606056
OpenAlexW2090467392

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.