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

The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.

Nature structural & molecular biology - 1 Mar 2008

Collins Robert E, Northrop Jeffrey P, Horton John R, Lee David Y, Zhang Xing, Stallcup Michael R, Cheng Xiaodong

Abstract excerpt

Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or...

Read the complete abstract on PubMed

Topics

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

Share to Ankyrin Repeat
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to COS Cells

Share to Histone-Lysine N-Methyltransferase

Share to Lysine

Share to Methylation

Share to Methyltransferases

Share to Mutant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 18264113
DOI: 10.1038/nsmb.1384
PMCID: PMC2586904

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.PMID 18264113Read ↗

Recognition of H3K9 methylation by GLP is required for efficient establishment of H3K9 methylation, rapid target gene repression, and mouse viability.Semantic proximity Read ↗

Automethylation of G9a and its implication in wider substrate specificity and HP1 binding.Semantic proximity Read ↗

G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription.Semantic proximity Read ↗

Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain.Semantic proximity Read ↗

Methylation of DNA Ligase 1 by G9a/GLP Recruits UHRF1 to Replicating DNA and Regulates DNA Methylation.Semantic proximity Read ↗

Direct interrogation of the role of H3K9 in metazoan heterochromatin function.Semantic proximity Read ↗

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.Semantic proximity Read ↗

S-adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3.Semantic proximity Read ↗

Histone tails regulate DNA methylation by allosterically activating de novo methyltransferase.Semantic proximity Read ↗

A role for the arginine methylation of Rad9 in checkpoint control and cellular sensitivity to DNA damage.Semantic proximity Read ↗

Evolutionary adaptation of the fly Pygo PHD finger toward recognizing histone H3 tail methylated at arginine 2.Semantic proximity Read ↗

Drosophila G9a is a nonessential gene.Semantic proximity Read ↗

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