Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Histone H3 lysine 56 acetylation and the response to DNA replication fork damage.

Molecular and cellular biology - 1 Jan 2012

Wurtele Hugo, Kaiser Gitte Schalck, Bacal Julien, St-Hilaire Edlie, Lee Eun-Hye, Tsao Sarah, Dorn Jonas, Maddox Paul, Lisby Michael, Pasero Philippe, Verreault Alain

Abstract excerpt

In Saccharomyces cerevisiae, histone H3 lysine 56 acetylation (H3K56ac) occurs in newly synthesized histones that are deposited throughout the genome during DNA replication. Defects in H3K56ac sensitize cells to genotoxic agents, suggesting that this modification plays an important role in the DNA damage response. However, the links between histone acetylation, the nascent chromatin structure, and the DNA damage...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylation
Share to Camptothecin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Replication

Share to Histones

Share to Hydroxyurea

Share to Lysine

Share to Methyl Methanesulfonate

Share to Mutagens

Source

Open in PubMed Open full text

Identifiers

PMID: 22025679
DOI: 10.1128/MCB.05415-11
PMCID: PMC3255698

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Histone H3 lysine 56 acetylation and the response to DNA replication fork damage.PMID 22025679Read ↗

Histone H3K56 acetylation, CAF1, and Rtt106 coordinate nucleosome assembly and stability of advancing replication forks.Semantic proximity Read ↗

Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae.Semantic proximity Read ↗

Persistent Acetylation of Histone H3 Lysine 56 Compromises the Activity of DNA Replication Origins.Semantic proximity Read ↗

Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis.Semantic proximity Read ↗

Hst3 is regulated by Mec1-dependent proteolysis and controls the S phase checkpoint and sister chromatid cohesion by deacetylating histone H3 at lysine 56.Semantic proximity Read ↗

Histone H3 K56 hyperacetylation perturbs replisomes and causes DNA damage.Semantic proximity Read ↗

Hyper-Acetylation of Histone H3K56 Limits Break-Induced Replication by Inhibiting Extensive Repair Synthesis.Semantic proximity Read ↗

A negatively charged residue in place of histone H3K56 supports chromatin assembly factor association but not genotoxic stress resistance.Semantic proximity Read ↗

Proliferating cell nuclear antigen and ASF1 modulate silent chromatin in Saccharomyces cerevisiae via lysine 56 on histone H3.Semantic proximity Read ↗

ATP-dependent chromatin remodeling and histone acetyltransferases in 5-FU cytotoxicity in Saccharomyces cerevisiae.Semantic proximity Read ↗

Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly.Semantic proximity Read ↗

A reversible histone H3 acetylation cooperates with mismatch repair and replicative polymerases in maintaining genome stability.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.