ArticleScientific reports2016
Extended string-like binding of the phosphorylated HP1α N-terminal tail to the lysine 9-methylated histone H3 tail.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Dynamic networks of intrinsically disordered regions in nuclear proteins.Biophysics and physicobiology · 2026Article
- Revealing site-specific molecular features mediating contacts of heterochromatin protein 1 α (HP1α) and the interactions with chromatin and DNA in LLPS environments.Communications biology · 2025Article
- Review
- A dynamic structural unit of phase-separated heterochromatin protein 1α as revealed by integrative structural analyses.Nucleic acids research · 2025Article
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes.Nature communications · 2021Article
- "Protein" no longer means what it used to.Current research in structural biology · 2021Review
- How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance.Cells · 2020Review
- Heterochromatin protein 1 (HP1): interactions with itself and chromatin components.Biophysical reviews · 2020Review
- Structural visualization of key steps in nucleosome reorganization by human FACT.Scientific reports · 2019Article
- Interactions of HP1 Bound to H3K9me3 Dinucleosome by Molecular Simulations and Biochemical Assays.Biophysical journal · 2018Article
- Diversification of HP1-like Chromo Domain Proteins in Tetrahymena thermophila.The Journal of eukaryotic microbiology · 2018Article
- Single-molecule kinetic analysis of HP1-chromatin binding reveals a dynamic network of histone modification and DNA interactions.Nucleic acids research · 2017Article
- The effect of epigenetic modifications on the secondary structures and possible binding positions of the N-terminal tail of histone H3 in the nucleosome: a computational study.Journal of molecular modeling · 2017Article
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11 authors.
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Abstract
The chromodomain of HP1α binds directly to lysine 9-methylated histone H3 (H3K9me). This interaction is enhanced by phosphorylation of serine residues in the N-terminal tail of HP1α by unknown mechanism. Here we show that phosphorylation modulates flexibility of HP1α's N-terminal tail, which strengthens the interaction with H3. NMR analysis of HP1α's chromodomain with N-terminal tail reveals that phosphorylation does not change the overall tertiary structure, but apparently reduces the tail dynamics. Small angle X-ray scattering confirms that phosphorylation contributes to extending HP1α's N-terminal tail. Systematic analysis using deletion mutants and replica exchange molecular dynamics simulations indicate that the phosphorylated serines and following acidic segment behave like an extended string and dynamically bind to H3 basic residues; without phosphorylation, the most N-terminal basic segment of HP1α inhibits interaction of the acidic segment with H3. Thus, the dynamic string-like behavior of HP1α's N-terminal tail underlies the enhancement in H3 binding due to phosphorylation.
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