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

Combined Interactions of Plant Homeodomain and Chromodomain Regulate NuA4 Activity at DNA Double-Strand Breaks.

Genetics - 1 Jan 2016

Su Wen-Pin, Hsu Sen-Huei, Chia Li-Chiao, Lin Jui-Yang, Chang Song-Bin, Jiang Zong-da, Lin Yi-Ju, Shih Min-Yu, Chen Yi-Cheng, Chang Mau-Sun, Yang Wen-Bin, Hung Jan-Jong, Hung Po-Cheng, Wu Wei-Sheng, Myung Kyungjae, Liaw Hungjiun

Abstract excerpt

DNA double-strand breaks (DSBs) represent one of the most threatening lesions to the integrity of genomes. In yeast Saccharomyces cerevisiae, NuA4, a histone acetylation complex, is recruited to DSBs, wherein it acetylates histones H2A and H4, presumably relaxing the chromatin and allowing access to repair proteins. Two subunits of NuA4, Yng2 and Eaf3, can interact in vitro with methylated H3K4 and H3K36 via...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Acetyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bleomycin

Share to Chromatin

Share to DNA Breaks, Double-Stranded

Share to Drug Resistance, Fungal

Share to Histone Acetyltransferases

Share to Methylation

Source

Open in PubMed Open full text

Identifiers

PMID: 26564157
DOI: 10.1534/genetics.115.184432
PMCID: PMC4701104

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Combined Interactions of Plant Homeodomain and Chromodomain Regulate NuA4 Activity at DNA Double-Strand Breaks.PMID 26564157Read ↗

A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation.Semantic proximity Read ↗

NuA4 links methylation of histone H3 lysines 4 and 36 to acetylation of histones H4 and H3.Semantic proximity Read ↗

NuA4 lysine acetyltransferase Esa1 is targeted to coding regions and stimulates transcription elongation with Gcn5.Semantic proximity Read ↗

The Transcriptional Coactivator ADA2b Recruits a Structural Maintenance Protein to Double-Strand Breaks during DNA Repair in Plants.Semantic proximity Read ↗

Regulation of NuA4 histone acetyltransferase activity in transcription and DNA repair by phosphorylation of histone H4.Semantic proximity Read ↗

Arabidopsis Histone Variant H2A.X Functions in the DNA Damage-Coupling Abscisic Acid Signaling Pathway.Semantic proximity Read ↗

Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4.Semantic proximity Read ↗

Piccolo NuA4-catalyzed acetylation of nucleosomal histones: critical roles of an Esa1 Tudor/chromo barrel loop and an Epl1 enhancer of polycomb A (EPcA) basic region.Semantic proximity Read ↗

Histone H3 K36 methylation is mediated by a trans-histone methylation pathway involving an interaction between Set2 and histone H4.Semantic proximity Read ↗

Overexpression of Eaf1, a subunit of the NuA4 lysine acetyltransferase complex, rescues growth defects in the <i>Saccharomyces cerevisiae</i> H3K36M oncohistone model via histone H4 tail acetylationSemantic proximity Read ↗

Novel trans-tail regulation of H2B ubiquitylation and H3K4 methylation by the N terminus of histone H2A.Semantic proximity Read ↗

AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex.Semantic proximity Read ↗

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