Evidence map›Paper›PMID 17283062›Full record

ArticleMolecular and cellular biology2007

Identification of Rkr1, a nuclear RING domain protein with functional connections to chromatin modification in Saccharomyces cerevisiae.

Mary A Braun, Patrick J Costa, Elia M Crisucci, Karen M Arndt

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Conservation and Expansion of Transcriptional Factor Repertoire in thebioRxiv : the preprint server for biology · 2023
    Article
  3. Article
  4. Review
  5. Review
  6. Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion.International journal of molecular sciences · 2020
    Review
  7. 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

4 authors at 1 institution in 1 country.

Mary A BraunDepartment of Biological Sciences, University of Pittsburgh, 269 Crawford Hall, 4249 Fifth Avenue, Pittsburgh, PA 15260, USA.
Patrick J Costa
Elia M Crisucci
Karen M Arndt
University of Pittsburgh · US

Funding

TRANSCRIPTION FACTOR MUTANTS OF YEASTR01GM052593 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ARNDT, KAREN M · 1995 to 2020
$7.9M
NIGMS NIH HHS GM52593NIGMS NIH HHS R01 GM052593
6 · The paper itself

Abstract

Proper transcription by RNA polymerase II is dependent on the modification state of the chromatin template. The Paf1 complex is associated with RNA polymerase II during transcription elongation and is required for several histone modifications that mark active genes. To uncover additional factors that regulate chromatin or transcription, we performed a genetic screen for mutations that cause lethality in the absence of the Paf1 complex component Rtf1. Our results have led to the discovery of a previously unstudied gene, RKR1. Strains lacking RKR1 exhibit phenotypes associated with defects in transcription and chromatin function. These phenotypes include inositol auxotrophy, impaired telomeric silencing, and synthetic lethality with mutations in SPT10, a gene that encodes a putative histone acetyltransferase. In addition, deletion of RKR1 causes severe genetic interactions with mutations that prevent histone H2B lysine 123 ubiquitylation or histone H3 lysine 4 methylation. RKR1 encodes a conserved nuclear protein with a functionally important RING domain at its carboxy terminus. In vitro experiments indicate that Rkr1 possesses ubiquitin-protein ligase activity. Taken together, our results identify a new participant in a protein ubiquitylation pathway within the nucleus that acts to modulate chromatin function and transcription.

Indexed as

Amino Acid SequenceChromatinConserved SequenceGenes, FungalGene SilencingHistone AcetyltransferasesMolecular Sequence DataNuclear ProteinsProtein Structure, TertiaryProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTelomereTranscription FactorsChromatinHistone AcetyltransferasesNuclear ProteinsRecombinant Fusion ProteinsRkr1 protein, S cerevisiaeRTF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPT10 protein, S cerevisiaeTATA-Box Binding ProteinTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID17283062
PMCPMC1899926
OpenAlexW2111064340

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.