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 H4 K16Q mutation, an acetylation mimic, causes structural disorder of its N-terminal basic patch in the nucleosome.

Journal of molecular biology - 3 Aug 2012

Zhou Bing-Rui, Feng Hanqiao, Ghirlando Rodolfo, Kato Hidenori, Gruschus James, Bai Yawen

Abstract excerpt

Histone tails and their posttranslational modifications play important roles in regulating the structure and dynamics of chromatin. For histone H4, the basic patch K(16)R(17)H(18)R(19) in the N-terminal tail modulates chromatin compaction and nucleosome sliding catalyzed by ATP-dependent ISWI chromatin remodeling enzymes while acetylation of H4 K16 affects both functions. The structural basis for the effects of...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Chromatin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromatin Assembly and Disassembly

Share to Histones

Share to Lysine

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Nucleosomes

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 22575889
DOI: 10.1016/j.jmb.2012.04.032
PMCID: PMC3392517

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

Histone H4 K16Q mutation, an acetylation mimic, causes structural disorder of its N-terminal basic patch in the nucleosome.PMID 22575889Read ↗

Hierarchical Anchoring–Gating Dictates Specific H4K16 Acetylation by the Human MSL ComplexSemantic proximity Read ↗

Differential contributions of histone H3 and H4 residues to heterochromatin structure.Semantic proximity Read ↗

The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association.Semantic proximity Read ↗

Mutations in non-acid patch residues disrupt H2A.Z's association with chromatin through multiple mechanisms.Semantic proximity Read ↗

Behaviors of nucleosomes with mutant histone H4s in euchromatic domains of living human cells.Semantic proximity Read ↗

Structural and thermodynamic impact of oncogenic mutations on the nucleosome core particle.Semantic proximity Read ↗

Comprehensive structural analysis of mutant nucleosomes containing lysine to glutamine (KQ) substitutions in the H3 and H4 histone-fold domains.Semantic proximity Read ↗

Capturing Snapshots of Nucleosomal H2A K13/K15 Ubiquitination Mediated by the Monomeric E3 Ligase RNF168Semantic proximity Read ↗

Molecular mechanism of histone variant H2A.B on stability and assembly of nucleosome and chromatin structures.Semantic proximity Read ↗

Behaviors of nucleosomes with mutant histone H4s in euchromatic domains of living human cellsSemantic proximity Read ↗

Nucleosome-CHD4 chromatin remodeller structure explains human disease mutationsSemantic proximity Read ↗

NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53.Semantic proximity Read ↗

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