Evidence map›Paper›PMID 19578373›Full record

ArticleNature cell biology2009

Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis.

Rakesh Kumar Singh, Marie-Helene Miquel Kabbaj, Johanna Paik, Akash Gunjan

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

129 citing papers in PubMed, 206 citations in OpenAlex.

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  7. Reevaluation of whether histones are asymmetrically segregated during asymmetric divisions of stem cells inProceedings of the National Academy of Sciences of the United States of America · 2025
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69 more citing papers are in PubMed but not listed here.

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.

Rakesh Kumar SinghDepartment of Biomedical Sciences, College of Medicine, Florida State University, 1115 West Call Street, Tallahassee, FL 32306-4300, USA.
Marie-Helene Miquel Kabbaj
Johanna Paik
Akash Gunjan
Florida State University · US

Funding

Regulation of histone genes upon replication arrest and DNA damage R15GM079678 · NIGMS · FLORIDA STATE UNIVERSITY · PI PAIK, HYERYUN JOHANNA · 2007 to 2007
$215k
NIGMS NIH HHS R15 GM079678NIGMS NIH HHS R15GM079678-01
6 · The paper itself

Abstract

Histone levels are tightly regulated to prevent harmful effects such as genomic instability and hypersensitivity to DNA-damaging agents due to the accumulation of these highly basic proteins when DNA replication slows down or stops. Although chromosomal histones are stable, excess (non-chromatin bound) histones are rapidly degraded in a Rad53 (radiation sensitive 53) kinase-dependent manner in Saccharomyces cerevisiae. Here we demonstrate that excess histones associate with Rad53 in vivo and seem to undergo modifications such as tyrosine phosphorylation and polyubiquitylation, before their proteolysis by the proteasome. We have identified the Tyr 99 residue of histone H3 as being critical for the efficient ubiquitylation and degradation of this histone. We have also identified the ubiquitin conjugating enzymes (E2) Ubc4 and Ubc5, as well as the ubiquitin ligase (E3) Tom1 (temperature dependent organization in mitotic nucleus 1), as enzymes involved in the ubiquitylation of excess histones. Regulated histone proteolysis has major implications for the maintenance of epigenetic marks on chromatin, genomic stability and the packaging of sperm DNA.

Indexed as

Blotting, WesternCell Cycle ProteinsCheckpoint Kinase 2Chromatin Assembly Factor-1Chromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistonesHydrolysisImmunoprecipitationMolecular ChaperonesMutationPhosphorylationProteasome Endopeptidase ComplexProtein BindingProtein Serine-Threonine KinasesSaccharomyces cerevisiaeASF1 protein, S cerevisiaeCell Cycle ProteinsCheckpoint Kinase 2Chromatin Assembly Factor-1Chromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistonesMolecular ChaperonesProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTOM1 protein, S cerevisiaeTyrosineUbc4 protein, S cerevisiaeUBC5 protein, S cerevisiaeUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID19578373
PMCPMC2720428
OpenAlexW1985188792

What OpenQuestion holds

Textmetadata
LicenceTDM
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.