Evidence map›Paper›PMID 18682387›Full record

ArticleThe Journal of biological chemistry2008

Dissection of coactivator requirement at RNR3 reveals unexpected contributions from TFIID and SAGA.

Hesheng Zhang, Jennifer A Kruk, Joseph C Reese

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 16 citations in OpenAlex.

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  15. Ccr4-Not complex: the control freak of eukaryotic cells.Critical reviews in biochemistry and molecular biology
    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

3 authors at 1 institution in 1 country.

Hesheng ZhangDepartment of Biochemistry and Molecular Biology, Center for Gene Regulation, Pennsylvania State University, University Park, Pennsylvania 16802.
Jennifer A KrukDepartment of Biochemistry and Molecular Biology, Center for Gene Regulation, Pennsylvania State University, University Park, Pennsylvania 16802.
Joseph C ReeseDepartment of Biochemistry and Molecular Biology, Center for Gene Regulation, Pennsylvania State University, University Park, Pennsylvania 16802. Electronic address: Jcr8@psu.edu.
Pennsylvania State University · US

Funding

REGULATION OF DNA DAMAGE INDUCED GENES BY YEAST TAFIISR01GM058672 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI REESE, JOSEPH C · 1999 to 2019
$6.5M
NIGMS NIH HHS GM58672NIGMS NIH HHS R01 GM058672
6 · The paper itself

Abstract

The gene encoding ribonucleotide reductase 3 (RNR3) is strongly induced in response to DNA damage. Its expression is strictly dependent upon the TAF(II) subunits of TFIID, which are required for the recruitment of SWI/SNF and nucleosome remodeling. However, full activation of RNR3 also requires GCN5, the catalytic subunit of the SAGA histone acetyltransferase complex. Thus, RNR3 is dependent upon both TFIID and SAGA, two complexes that deliver TATA-binding protein (TBP) to promoters. Furthermore, unlike the majority of TFIID-dominated genes, RNR3 contains a consensus TATA-box, a feature of SAGA-regulated core promoters. Although a large fraction of the genome can be characterized as either TFIID- or SAGA-dominant, it is expected that many genes utilize both. The mechanism of activation and the relative contributions of SAGA and TFIID at genes regulated by both complexes have not been examined. Here we delineated the role of SAGA in the regulation of RNR3 and contrast it to that of TFIID. We find that SAGA components fulfill distinct functions in the regulation of RNR3. The core promoter of RNR3 is SAGA-dependent, and we provide evidence that SAGA, not TAF(II)s within TFIID, are largely responsible for TBP recruitment. This taken together with our previous work provides evidence that SAGA recruits TBP, whereas TFIID mediates chromatin remodeling. Thus, we described an unexpected shift in the division of labor between these two complexes and provide the first characterization of a gene that requires both SAGA and TFIID.

Indexed as

Cell Cycle ProteinsChromatin Assembly and DisassemblyDNA DamageGene Expression Regulation, EnzymologicGene Expression Regulation, FungalGenome, FungalHistone AcetyltransferasesNuclear ProteinsNucleosomesp300-CBP-Associated FactorRibonucleoside Diphosphate ReductaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTrans-ActivatorsCell Cycle ProteinsGCN5 protein, S cerevisiaeHistone AcetyltransferasesNuclear ProteinsNucleosomesp300-CBP-Associated FactorRibonucleoside Diphosphate ReductaseRNR3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeSPT15 protein, S cerevisiaeSWI3 protein, S cerevisiaeTAF2 protein, S cerevisiaeTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTrans-ActivatorsTranscription Factor TFIID

Identifiers

PMID18682387
PMCPMC2562059
OpenAlexW2092923920

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.