Evidence map›Paper›PMID 19536766›Full record

ArticleYeast (Chichester, England)2009

Identification of proteins associated with the yeast mitochondrial RNA polymerase by tandem affinity purification.

Dmitriy A Markov, Maria Savkina, Michael Anikin, Mark Del Campo, Karen Ecker, Alan M Lambowitz, Jon P De Gnore, William T McAllister

Open access · bronzeAbstract read
In one paragraph

Article in Yeast (Chichester, England), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The pentatricopeptide repeat protein Rmd9 recognizes the dodecameric element in the 3'-UTRs of yeast mitochondrial mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Review
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  7. AEMBO reports · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

8 authors at 4 institutions in 1 country.

Dmitriy A MarkovDepartments of Cell Biology, University of Medicine and Dentistry of New Jersey, Stratford, USA. markovdm@umdnj.edu
Maria Savkina
Michael Anikin
Mark Del Campo
Karen Ecker
Alan M Lambowitz
Jon P De Gnore
William T McAllister
Stratford University · USRowan University · USThe University of Texas at Austin · USTufts University · US

Funding

RNA SPLICING IN NEUROSPORA MITOCHONDRIAR01GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1986 to 2016
$6.6M
RNA POLYMERASE STRUCTURE/FUNCTIONR01GM038147 · NIGMS · UNIV OF MED/DENT NJ-SCH OSTEOPATHIC MED · PI MCALLISTER, WILLIAM T · 1986 to 2007
$3.5M
INVOLVEMENT OF PROTEINS IN SPLICING GROUP I INTRONSR37GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1993 to 2002
$1.2M
Structure and function of a DEAD-box protein in group I intron splicingF32GM076961 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI DEL CAMPO, MARK · 2006 to 2008
$145k
NIGMS NIH HHS F32 GM076961NIGMS NIH HHS F32-GM76961NIGMS NIH HHS GM037951NIGMS NIH HHS GM38147NIGMS NIH HHS R01 GM037951NIGMS NIH HHS R01 GM038147NIGMS NIH HHS R37 GM037951
6 · The paper itself

Abstract

The abundance of mitochondrial (mt) transcripts varies under different conditions, and is thought to depend upon rates of transcription initiation, transcription termination/attenuation and RNA processing/degradation. The requirement to maintain the balance between RNA synthesis and processing may involve coordination between these processes; however, little is known about factors that regulate the activity of mtRNA polymerase (mtRNAP). Recent attempts to identify mtRNAP-protein interactions in yeast by means of a generalized tandem affinity purification (TAP) protocol were not successful, most likely because they involved a C-terminal mtRNAP-TAP fusion (which is incompatible with mtRNAP function) and because of the use of whole-cell solubilization protocols that did not preserve the integrity of mt protein complexes. Based upon the structure of T7 RNAP (to which mtRNAPs show high sequence similarity), we identified positions in yeast mtRNAP that allow insertion of a small affinity tag, confirmed the mature N-terminus, constructed a functional N-terminal TAP-mtRNAP fusion, pulled down associated proteins, and identified them by LC-MS-MS. Among the proteins found in the pull-down were a DEAD-box protein (Mss116p) and an RNA-binding protein (Pet127p). Previous genetic experiments suggested a role for these proteins in linking transcription and RNA degradation, in that a defect in the mt degradadosome could be suppressed by overexpression of either of these proteins or, independently, by mutations in either mtRNAP or its initiation factor Mtf1p. Further, we found that Mss116p inhibits transcription by mtRNAP in vitro in a steady-state reaction. Our results support the hypothesis that Mss116p and Pet127p are involved in modulation of mtRNAP activity.

Indexed as

Amino Acid SequenceChromatography, AffinityChromatography, LiquidDNA-Directed RNA PolymerasesGTP-Binding ProteinsMitochondriaMitochondrial ProteinsModels, MolecularMolecular Sequence DataProtein Structure, TertiaryRNARNA, FungalRNA, MitochondrialSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidDNA-Directed RNA PolymerasesGTP-Binding ProteinsMitochondrial ProteinsMSS1 protein, S cerevisiaePET127 protein, S cerevisiaeRNARNA, FungalRNA, MitochondrialSaccharomyces cerevisiae Proteins

Identifiers

PMID19536766
PMCPMC2896726
OpenAlexW2025484266

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.