Evidence map›Paper›PMID 22564898›Full record

ArticleNucleic acids research2012

A genetic screen for terminator function in yeast identifies a role for a new functional domain in termination factor Nab3.

Travis J Loya, Thomas W O'Rourke, Daniel Reines

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Travis J LoyaDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
Thomas W O'Rourke
Daniel Reines
Emory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
RNA POLYMERASE II ELONGATION COMPLEX--STRUCTURE/FUNCTIONR01GM046331 · NIGMS · EMORY UNIVERSITY · PI REINES, DANIEL · 1991 to 2013
$3.5M
NIGMS NIH HHS GM46331NIGMS NIH HHS R01 GM046331NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

The yeast IMD2 gene encodes an enzyme involved in GTP synthesis. Its expression is controlled by guanine nucleotides through a set of alternate start sites and an intervening transcriptional terminator. In the off state, transcription results in a short non-coding RNA that starts upstream of the gene. Transcription terminates via the Nrd1-Nab3-Sen1 complex and is degraded by the nuclear exosome. Using a sensitive terminator read-through assay, we identified trans-acting Terminator Override (TOV) genes that operate this terminator. Four genes were identified: the RNA polymerase II phosphatase SSU72, the RNA polymerase II binding protein PCF11, the TRAMP subunit TRF4 and the hnRNP-like, NAB3. The TOV phenotype can be explained by the loss of function of these gene products as described in models in which termination and RNA degradation are coupled to the phosphorylation state of RNA polymerase II's repeat domain. The most interesting mutations were those found in NAB3, which led to the finding that the removal of merely three carboxy-terminal amino acids compromised Nab3's function. This region of previously unknown function is distant from the protein's well-known RNA binding and Nrd1 binding domains. Structural homology modeling suggests this Nab3 'tail' forms an α-helical multimerization domain that helps assemble it onto an RNA substrate.

Indexed as

Transcription, GeneticAllelesAmino Acid SequenceCell SeparationDNA-Directed DNA PolymeraseFlow CytometryIMP DehydrogenaseMolecular Sequence DataMutationNuclear ProteinsProtein Structure, TertiaryRNARNA-Binding ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Directed DNA PolymeraseIMD2 protein, S cerevisiaeIMP DehydrogenaseNAB3 protein, S cerevisiaeNuclear ProteinsPAP2 protein, S cerevisiaeRNARNA-Binding ProteinsRNA Polymerase IISaccharomyces cerevisiae Proteins

Identifiers

PMID22564898
PMCPMC3424548
OpenAlexW2083837296

What OpenQuestion holds

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LicenceCC BY-NC
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.