Evidence map›Paper›PMID 11046131›Full record

ArticleMolecular and cellular biology2000

Functional interaction between Ssu72 and the Rpb2 subunit of RNA polymerase II in Saccharomyces cerevisiae.

D L Pappas, M Hampsey

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Dephosphorylating eukaryotic RNA polymerase II.Biochimica et biophysica acta · 2016
    Review
  17. Article
  18. Article
  19. Article
  20. Review
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.

D L PappasDepartment of Biochemistry, Division of Nucleic Acids Enzymology, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
M Hampsey
Johnson University · US

Funding

GENETIC ANALYSIS OF TRANSCRIPTION INITIATION IN YEASTR01GM039484 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI HAMPSEY, MICHAEL · 1995 to 2012
$2.7M
GENETIC ANALYSIS OF TRANSLATION INITIATION IN YEASTR29GM039484 · NIGMS · LOUISIANA STATE UNIV HSC SHREVEPORT · PI HAMPSEY, MICHAEL · 1988 to 1993
–
NIGMS NIH HHS GM39484NIGMS NIH HHS R01 GM039484
6 · The paper itself

Abstract

SSU72 is an essential gene encoding a phylogenetically conserved protein of unknown function that interacts with the general transcription factor TFIIB. A recessive ssu72-1 allele was identified as a synthetic enhancer of a TFIIB (sua7-1) defect, resulting in a heat-sensitive (Ts(-)) phenotype and a dramatic downstream shift in transcription start site selection. Here we describe a new allele, ssu72-2, that confers a Ts(-) phenotype in a SUA7 wild-type background. In an effort to further define Ssu72, we isolated suppressors of the ssu72-2 mutation. One suppressor is allelic to RPB2, the gene encoding the second-largest subunit of RNA polymerase II (RNAP II). Sequence analysis of the rpb2-100 suppressor defined a cysteine replacement of the phylogenetically invariant arginine residue at position 512 (R512C), located within homology block D of Rpb2. The ssu72-2 and rpb2-100 mutations adversely affected noninduced gene expression, with no apparent effects on activated transcription in vivo. Although isolated as a suppressor of the ssu72-2 Ts(-) defect, rpb2-100 enhanced the transcriptional defects associated with ssu72-2. The Ssu72 protein interacts directly with purified RNAP II in a coimmunoprecipitation assay, suggesting that the genetic interactions between ssu72-2 and rpb2-100 are a consequence of physical interactions. These results define Ssu72 as a highly conserved factor that physically and functionally interacts with the RNAP II core machinery during transcription initiation.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceCarrier ProteinsConserved SequenceFungal ProteinsMolecular Sequence DatamRNA Cleavage and Polyadenylation FactorsMutationPhosphoprotein PhosphatasesPhylogenyProtein SubunitsRNA Polymerase IISaccharomyces cerevisiaeSuppression, GeneticTranscription FactorsTranscription Factor TFIIBCarrier ProteinsFungal ProteinsmRNA Cleavage and Polyadenylation FactorsPhosphoprotein PhosphatasesProtein SubunitsRNA Polymerase IISaccharomyces cerevisiae ProteinsSSU72 protein, S cerevisiaeTranscription FactorsTranscription Factor TFIIB

Identifiers

PMID11046131
PMCPMC102141
OpenAlexW2132198636

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.