ArticleNucleic acids research2018
The interplay between H2A.Z and H3K9 methylation in regulating HP1α binding to linker histone-containing chromatin.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 62 citations in OpenAlex.
- Cooperative and Opposing Functions of ANP32E and VPS72 Govern Gene Promoter Chromatin Status.Research square · 2026Article
- Basis for lineage-determining pioneer factors targeting distinct repressed chromatin states.Science advances · 2026Article
- Role of noncanonical histone H2A variant, H2A.Z, to maintain proper centromeric transcription and chromosome segregation.The Journal of biological chemistry · 2025Article
- Integrated bioinformatics investigation and experimental validation reveals the clinical and biological significance of chromobox family in breast cancer.Scientific reports · 2025Article
- Multifunctional histone variants in genome function.Nature reviews. Genetics · 2025Review
- Structural mechanism of HP1⍺-dependent transcriptional repression and chromatin compaction.Structure (London, England : 1993) · 2024Article
- Epigenetic modulation via the C-terminal tail of H2A.Z.Nature communications · 2024Article
- Identification of a novel DNA oxidative damage repair pathway, requiring the ubiquitination of the histone variant macroH2A1.1.BMC biology · 2024Article
- Unveiling the role of HP1α-HDAC1-STAT1 axis as a therapeutic target for HP1α-positive intrahepatic cholangiocarcinoma.Journal of experimental & clinical cancer research : CR · 2024Article
- CFDP1 regulates the stability of pericentric heterochromatin thereby affecting RAN GTPase activity and mitotic spindle formation.PLoS biology · 2024Article
- Multimodal interactions drive chromatin phase separation and compaction.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Competition for H2A.Z underlies the developmental impacts of repetitive element de-repression.Development (Cambridge, England) · 2023Article
- A complex interplay between H2A.Z and HP1 isoforms regulates pericentric heterochromatin.Frontiers in cell and developmental biology · 2023Article
- The H2A.Z-KDM1A complex promotes tumorigenesis by localizing in the nucleus to promote SFRP1 promoter methylation in cholangiocarcinoma cells.BMC cancer · 2022Article
- Chromatin remodeler Dmp18 regulates apoptosis by controlling H2Av incorporation in Drosophila imaginal disc development.PLoS genetics · 2022Article
- The Role of the Histone Variant H2A.Z in Metazoan Development.Journal of developmental biology · 2022Review
- A novel SNF2 ATPase complex in Trypanosoma brucei with a role in H2A.Z-mediated chromatin remodelling.PLoS pathogens · 2022Article
- Coordinated changes in gene expression, H1 variant distribution and genome 3D conformation in response to H1 depletion.Nucleic acids research · 2022Article
- DNA sequence-dependent formation of heterochromatin nanodomains.Nature communications · 2022Article
- Non-redundant functions of H2A.Z.1 and H2A.Z.2 in chromosome segregation and cell cycle progression.EMBO reports · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the most intensively studied chromatin binding factors is HP1α. HP1α is associated with silenced, heterochromatic regions of the genome and binds to H3K9me3. While H3K9me3 is necessary for HP1α recruitment to heterochromatin, it is becoming apparent that it is not sufficient suggesting that additional factors are involved. One candidate proposed as a potential regulator of HP1α recruitment is the linker histone H1.4. Changes to the underlying make-up of chromatin, such as the incorporation of the histone variant H2A.Z, has also been linked with regulating HP1 binding to chromatin. Here, we rigorously dissected the effects of H1.4, H2A.Z and H3K9me3 on the nucleosome binding activity of HP1α in vitro employing arrays, mononucleosomes and nucleosome core particles. Unexpectedly, histone H1.4 impedes the binding of HP1α but strikingly, this inhibition is partially relieved by the incorporation of both H2A.Z and H3K9me3 but only in the context of arrays or nucleosome core particles. Our data suggests that there are two modes of interaction of HP1α with nucleosomes. The first primary mode is through interactions with linker DNA. However, when linker DNA is missing or occluded by linker histones, HP1α directly interacts with the nucleosome core and this interaction is enhanced by H2A.Z with H3K9me3.
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