ArticleChembiochem : a European journal of chemical biology2011
The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners.
Article in Chembiochem : a European journal of chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 65 citations in OpenAlex.
- In vitro reconstitution of heterochromatin compartments reveals the spontaneous formation of tunable liquid-liquid interfaces.Nucleic acids research · 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
- Hierarchical interactions between nucleolar and heterochromatin condensates are mediated by a dual-affinity protein.Nature cell biology · 2025Article
- Rapid compensatory evolution within a multiprotein complex preserves telomere integrity.Science (New York, N.Y.) · 2025Article
- Review
- Expanding the HP1a-binding consensus and molecular grammar for heterochromatin assembly.Nucleic acids research · 2025Article
- HP1 loses its chromatin clustering and phase separation function across evolution.Nature communications · 2025Article
- Characterization of the Swi6/HP1 binding motif in its partner protein reveals the basis for the functional divergence of the HP1 family proteins in fission yeast.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- HP1a promotes chromatin liquidity and drives spontaneous heterochromatin compartmentalization.bioRxiv : the preprint server for biology · 2025Article
- Structural mechanism of HP1⍺-dependent transcriptional repression and chromatin compaction.Structure (London, England : 1993) · 2024Article
- Relationship between lysine methyltransferase levels and heterochromatin gene repression in living cells and in silico.PNAS nexus · 2023Article
- Article
- CEBIT screening for inhibitors of the interaction between SARS-CoV-2 spike and ACE2.Fundamental research · 2022Article
- Discovery of Potent Peptidomimetic Antagonists for Heterochromatin Protein 1 Family Proteins.ACS omega · 2022Article
- Insights into HP1a-Chromatin Interactions.Cells · 2020Review
- Heterochromatin protein 1 (HP1): interactions with itself and chromatin components.Biophysical reviews · 2020Review
- NBS1 interacts with HP1 to ensure genome integrity.Cell death & disease · 2019Article
- KDM2A-dependent reduction of rRNA transcription on glucose starvation requires HP1 in cells, including triple-negative breast cancer cells.Oncotarget · 2019Article
- Biophysical Properties of HP1-Mediated Heterochromatin.Cold Spring Harbor symposia on quantitative biology · 2019Article
- Structural insights into Rhino-Deadlock complex for germline piRNA cluster specification.EMBO reports · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Drosophila melanogaster heterochromatin protein 1a (HP1a) is essential for compacted heterochromatin structure and the associated gene silencing. Its chromo shadow domain (CSD) is well known for binding to peptides that contain a PXVXL motif. Heterochromatin protein 2 (HP2) is a non-histone chromosomal protein that associates with HP1a in the pericentric heterochromatin, telomeres, and the fourth chromosome. Using NMR spectroscopy, fluorescence polarization, and site-directed mutagenesis, we identified an LCVKI motif in HP2 that binds to the HP1a CSD. The binding affinity of the HP2 fragment is approximately two orders of magnitude higher than that of peptides from PIWI (with a PRVKV motif), AF10 (with a PLVVL motif), or CG15356 (with LYPLL and LSIVA motifs). To delineate differential interactions of the HP1a CSD, we characterized its structure, backbone dynamics, and dimerization constant. We found that the dimerization constant is bracketed by the affinities of HP2 and PIWI, which dock to the same HP1a homodimer surface. This suggests that HP2, but not PIWI, interaction can drive the homodimerization of HP1a. Interestingly, the integrity of the disordered C-terminal extension (CTE) of HP1a is essential for discriminatory binding, whereas swapping the PXVXL motifs does not confer specificity. Serine phosphorylation at the peptide binding surface of the CSD is thought to regulate heterochromatin assembly. Glutamic acid substitution at these sites destabilizes HP1a dimers, but improves the interaction with both binding partners. Our studies underscore the importance of CSD dimerization and cooperation with the CTE in forming distinct complexes of HP1a.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.