Evidence map›Paper›PMID 11486042›Full record

ArticleMolecular and cellular biology2001

Partners of Rpb8p, a small subunit shared by yeast RNA polymerases I, II and III.

J F Briand, F Navarro, P Rematier, C Boschiero, S Labarre, M Werner, G V Shpakovski, P Thuriaux

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

8 authors.

J F BriandService de Biochimie and Génétique Moléculaire, CEA/Saclay, F-91191 Gif-sur-Yvette, France.
F Navarro
P Rematier
C Boschiero
S Labarre
M Werner
G V Shpakovski
P Thuriaux

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rpb8p, a subunit common to the three yeast RNA polymerases, is conserved among eukaryotes and absent from noneukaryotes. Defective mutants were found at an invariant GGLLM motif and at two other highly conserved amino acids. With one exception, they are clustered on the Rpb8p structure. They all impair a two-hybrid interaction with a fragment conserved in the largest subunits of RNA polymerases I (Rpa190p), II (Rpb1p), and III (Rpc160p). This fragment corresponds to the pore 1 module of the RNA polymerase II crystal structure and bears a highly conserved motif (P.I.KP.LW.GKQ) facing the GGLLM motif of Rpb8p. An RNA polymerase I mutant (rpa190-G728D) at the invariant glycyl of P.I.KP.LW.GKQ provokes a temperature-sensitive defect. Increasing the gene dosage of another common subunit, Rpb6p, suppresses this phenotype. It also suppresses a conditional growth defect observed when replacing Rpb8p by its human counterpart. Hence, Rpb6p and Rpb8p functionally interact in vivo. These two subunits are spatially separated by the pore 1 module and may also be possibly connected by the disorganized N half of Rpb6p, not included in the present structure data. Human Rpb6p is phosphorylated at its N-terminal Ser2, but an alanyl replacement at this position still complements an rpb6-Delta null allele. A two-hybrid interaction also occurs between Rpb8p and the product of orphan gene YGR089w. A ygr089-Delta null mutant has no detectable growth defect but aggravates the conditional growth defect of rpb8 mutants, suggesting that the interaction with Rpb8p may be physiologically relevant.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBinding SitesDNA-Directed RNA PolymerasesHumansModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, SecondaryProtein SubunitsRNA Polymerase IRNA Polymerase IIRNA Polymerase IIISaccharomyces cerevisiaeTwo-Hybrid System TechniquesDNA-Directed RNA PolymerasesProtein SubunitsRNA Polymerase IRNA Polymerase IIRNA Polymerase IIIRpb8 protein, S cerevisiaeRPO26 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID11486042
PMCPMC87322

What OpenQuestion holds

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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.