Evidence map›Paper›PMID 16020781›Full record

ArticleGenetics2005

Regulation of histone deposition proteins Asf1/Hir1 by multiple DNA damage checkpoint kinases in Saccharomyces cerevisiae.

Judith A Sharp, Gizem Rizki, Paul D Kaufman

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

27 citing papers in PubMed, 35 citations in OpenAlex.

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  12. Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction.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

3 authors at 3 institutions in 1 country.

Judith A SharpLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Gizem Rizki
Paul D Kaufman
Lawrence Berkeley National Laboratory · USUniversity of California, Berkeley · USUniversity of Massachusetts Chan Medical School · US

Funding

Regulation of repetitive chromatin structures during the human cell cycleR01GM055712 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KAUFMAN, PAUL D. · 1997 to 2014
$5.1M
NIGMS NIH HHS GM55712NIGMS NIH HHS R01 GM055712
6 · The paper itself

Abstract

CAF-1, Hir proteins, and Asf1 are histone H3/H4 binding proteins important for chromatin-mediated transcriptional silencing. We explored genetic and physical interactions between these proteins and S-phase/DNA damage checkpoint kinases in the budding yeast Saccharomyces cerevisiae. Although cells lacking checkpoint kinase Mec1 do not display defects in telomeric gene silencing, silencing was dramatically reduced in cells lacking both Mec1 and the Cac1 subunit of CAF-1. Silencing was restored in cac1Delta and cac1Delta mec1Delta cells upon deletion of Rad53, the kinase downstream of Mec1. Restoration of silencing to cac1Delta cells required both Hir1 and Asf1, suggesting that Mec1 counteracts functional sequestration of the Asf1/Hir1 complex by Rad53. Consistent with this idea, the degree of suppression of silencing defects by rad53 alleles correlated with effects on Asf1 binding. Furthermore, deletion of the Dun1 kinase, a downstream target of Rad53, also suppressed the silencing defects of cac1Delta cells and reduced the levels of Asf1 associated with Rad53 in vivo. Loss of Mec1 and Rad53 did not alter telomere lengths or Asf1 protein levels, nuclear localization, or chromosome association. We conclude that the Mec1 and Dun1 checkpoint kinases regulate the Asf1-Rad53 interaction and therefore affect the activity of the Asf1/Hir complex in vivo.

Indexed as

Cell Cycle ProteinsCheckpoint Kinase 2DNA DamageEpistasis, GeneticGene SilencingHistonesIntracellular Signaling Peptides and ProteinsMolecular ChaperonesMutationNuclear ProteinsProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsASF1 protein, S cerevisiaeCell Cycle ProteinsCheckpoint Kinase 2DUN1 protein, S cerevisiaeHIR1 protein, S cerevisiaeHistonesIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMolecular ChaperonesNuclear ProteinsProtein KinasesProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID16020781
PMCPMC1456847
OpenAlexW2137223145

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.