ArticleNucleic acids research2025
Phosphorylation of HP1/Swi6 relieves competition with Suv39/Clr4 on nucleosomes and enables H3K9 trimethyl spreading.
Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- MoCul4 assists MoKmt1 to catalyze H3K9 methylation and regulates the growth, development, and pathogenicity inVirulence · 2026Article
- Nuclear size and physical properties of the nucleoplasm are determined by colloid osmotic pressure at the nuclear envelope.bioRxiv : the preprint server for biology · 2026Article
- The role of electrostatic interactions in the phase separation of HP1α and its protein binding partners.bioRxiv : the preprint server for biology · 2026Article
- Histone 3 lysine 9 dimethylation by the G9a-GLP heterodimer requires intranucleosomal product reading.bioRxiv : the preprint server for biology · 2026Article
- Discrete Subdomains Establish Epigenetic Diversity in Subtelomeric Heterochromatin.bioRxiv : the preprint server for biology · 2025Article
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9 authors.
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Abstract
Heterochromatin formation in Schizosaccharomyces pombe requires the spreading of histone 3 (H3) Lysine 9 (K9) methylation (me) from nucleation centers by the H3K9 methylase, Suv39/Clr4, and the reader protein, HP1/Swi6. To accomplish this, Suv39/Clr4 and HP1/Swi6 have to associate with nucleosomes both nonspecifically, binding DNA, and octamer surfaces and specifically, via recognition of methylated H3K9 by their respective chromodomains. However, how both proteins avoid competition for the same nucleosomes in this process is unclear. Here, we show that phosphorylation tunes oligomerization and the nucleosome affinity of HP1/Swi6 such that it preferentially partitions onto Suv39/Clr4's trimethyl product rather than its unmethylated substrates. Preferential partitioning enables efficient conversion from di-to trimethylation on nucleosomes in vitro and H3K9me3 spreading in vivo. Together, our data suggest that phosphorylation of HP1/Swi6 creates a regime that increases oligomerization and relieves competition with the "read-write" mechanism of Suv39/Clr4, together promoting for productive heterochromatin spreading.
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