Evidence map›Paper›PMID 11459833›Full record

ArticleGenes & development2001

The set1Delta mutation unveils a novel signaling pathway relayed by the Rad53-dependent hyperphosphorylation of replication protein A that leads to transcriptional activation of repair genes.

V Schramke, H Neecke, V Brevet, Y Corda, G Lucchini, M P Longhese, E Gilson, V Géli

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2001. 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
–field-weighted citation impact
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, 43 citations in OpenAlex.

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  8. Mutagenesis of pairwise combinations of histone amino-terminal tails reveals functional redundancy in budding yeast.Proceedings of the National Academy of Sciences of the United States of America · 2012
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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 at 4 institutions in 2 countries.

V SchramkeLaboratoire D'Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie (IBSM), Centre National de la Recherche Scientifique (CNRS), 13402, Marseille, Cedex 20, France.
H Neecke
V Brevet
Y Corda
G Lucchini
M P Longhese
E Gilson
V Géli
Laboratoire de Biologie et Modélisation de la Cellule · FRCentre National de la Recherche Scientifique · FRInstitut de Biologie Structurale · FRUniversity of Milano-Bicocca · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SET domain proteins are present in chromosomal proteins involved in epigenetic control of transcription. The yeast SET domain protein Set1p regulates chromatin structure, DNA repair, and telomeric functions. We investigated the mechanism by which the absence of Set1p increases DNA repair capacities of checkpoint mutants. We show that deletion of SET1 induces a response relayed by the signaling kinase Rad53p that leads to the MEC1/TEL1-independent hyperphosphorylation of replication protein A middle subunit (Rfa2p). Consequently, the binding of Rfa2p to upstream repressing sequences (URS) of repair genes is decreased, thereby leading to their derepression. Our results correlate the set1Delta-dependent phosphorylation of Rfa2p with the transcriptional induction of repair genes. Moreover, we show that the deletion of the amino-terminal region of Rfa2p suppresses the sensitivity to ultraviolet radiation of a mec3Delta checkpoint mutant, abolishes the URS-mediated repression, and increases the expression of repair genes. This work provides an additional link for the role of Rfa2p in the regulation of the repair capacity of the cell and reveals a role for the phosphorylation of Rfa2p and unveils unsuspected connections between chromatin, signaling pathways, telomeres, and DNA repair.

Indexed as

Cell Cycle ProteinsCheckpoint Kinase 2DNA-Binding ProteinsDNA RepairDose-Response Relationship, RadiationFungal ProteinsGene SilencingHistone-Lysine N-MethyltransferaseIntracellular Signaling Peptides and ProteinsModels, GeneticPhosphorylationProtein BindingProtein Serine-Threonine KinasesReplication Protein ASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsCheckpoint Kinase 2DNA-Binding ProteinsFungal ProteinsHistone-Lysine N-MethyltransferaseIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMEC3 protein, S cerevisiaeProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeReplication Protein ASaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeTEL1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID11459833
PMCPMC312739
OpenAlexW2134018414

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.