Evidence map›Paper›PMID 12407181›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship to Rpb4-Rpb7 pol II subunits.

Gerald Peyroche, Erwann Levillain, Magali Siaut, Isabelle Callebaut, Patrick Schultz, Andre Sentenac, Michel Riva, Christophe Carles

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Crystallization of RNA polymerase I subcomplex A14/A43 by iterative prediction, probing and removal of flexible regions.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The RNA polymerase I transcription machinery.Biochemical Society symposium · 2006
    Review
  17. Article
  18. Article
  19. Architecture of initiation-competent 12-subunit RNA polymerase II.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  20. Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription.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

8 authors at 2 institutions in 1 country.

Gerald PeyrocheLaboratoire de Transcription des Gènes, Commissariat à l'Energie Atomique/Saclay, 91191 Gif sur Yvette Cedex, France.
Erwann Levillain
Magali Siaut
Isabelle Callebaut
Patrick Schultz
Andre Sentenac
Michel Riva
Christophe Carles
Sorbonne Université · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A43, an essential subunit of yeast RNA polymerase I (pol I), interacts with Rrn3, a class I general transcription factor required for rDNA transcription. The pol I-Rrn3 complex is the only form of enzyme competent for promoter-dependent transcription initiation. In this paper, using biochemical and genetic approaches, we demonstrate that the A43 polypeptide forms a stable heterodimer with the A14 pol I subunit and interacts with the common ABC23 subunit, the yeast counterpart of the omega subunit of bacterial RNA polymerase. We show by immunoelectronic microscopy that A43, ABC23, and A14 colocalize in the three-dimensional structure of the pol I, and we demonstrate that the presence of A43 is required for the stabilization of both A14 and ABC23 within the pol I. Because the N-terminal half of A43 is clearly related to the pol II Rpb7 subunit, we propose that the A43-A14 pair is likely the pol I counterpart of the Rpb7-Rpb4 heterodimer, although A14 distinguishes from Rpb4 by specific sequence and structure features. This hypothesis, combined with our structural data, suggests a new localization of Rpb7-Rpb4 subunits in the three-dimensional structure of yeast pol II.

Indexed as

Amino Acid SequenceDNA, RibosomalModels, MolecularMolecular Sequence DataProtein ConformationProtein SubunitsRNA Polymerase ISaccharomyces cerevisiaeSequence AlignmentSequence Homology, Amino AcidTranscription FactorsDNA, RibosomalProtein SubunitsRNA Polymerase ITranscription Factors

Identifiers

PMID12407181
PMCPMC137477
OpenAlexW2038280837

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.