ArticleThe Journal of biological chemistry2013
Heterochromatin Protein 1a (HP1a) partner specificity is determined by critical amino acids in the chromo shadow domain and C-terminal extension.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- The novel HP1a interactor Clump/CG30403 safeguards transposon silencing and reproductive resilience in thebioRxiv : the preprint server for biology · 2026Article
- 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
- Review
- Expanding the HP1a-binding consensus and molecular grammar for heterochromatin assembly.Nucleic acids research · 2025Article
- HP1a promotes chromatin liquidity and drives spontaneous heterochromatin compartmentalization.bioRxiv : the preprint server for biology · 2025Article
- Heterochromatic gene silencing controls CD4Nature communications · 2025Article
- Epigenetic memory is governed by an effector recruitment specificity toggle in Heterochromatin Protein 1.Nature communications · 2024Article
- HP1-driven phase separation recapitulates the thermodynamics and kinetics of heterochromatin condensate formation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Discovery of Potent Peptidomimetic Antagonists for Heterochromatin Protein 1 Family Proteins.ACS omega · 2022Article
- Insights into HP1a-Chromatin Interactions.Cells · 2020Review
- 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
- piRNA-Guided Genome Defense: From Biogenesis to Silencing.Annual review of genetics · 2018Review
- Somatic role of SYCE2: an insulator that dissociates HP1α from H3K9me3 and potentiates DNA repair.Life science alliance · 2018Article
- Diversification of HP1-like Chromo Domain Proteins in Tetrahymena thermophila.The Journal of eukaryotic microbiology · 2018Article
- Engineered holocytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Arabidopsis DNA polymerase ϵ recruits components of Polycomb repressor complex to mediate epigenetic gene silencing.Nucleic acids research · 2016Article
- Heterochromatin-Associated Proteins HP1a and Piwi Collaborate to Maintain the Association of Achiasmate Homologs in Drosophila Oocytes.Genetics · 2016Article
- TALE-light imaging reveals maternally guided, H3K9me2/3-independent emergence of functional heterochromatin in Drosophila embryos.Genes & development · 2016Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Drosophila melanogaster Heterochromatin Protein 1a (HP1a) is an essential protein critical for heterochromatin assembly and regulation. Its chromo shadow domain (CSD) homodimerizes, a requirement for binding protein partners that contain a PXVXL motif. How does HP1a select among its many different PXVXL-containing partners? HP1a binds tightly to Heterochromatin Protein 2 (HP2), but weakly to PIWI. We investigated differences in homodimerization and the impact of the C-terminal extension (CTE) by contrasting HP1a to its paralogue, HP1b. HP1a and HP1b differ in the dimerization interface, with HP1a having an Arg at position 188 rather than Glu. We find that while this substitution reduces the dimerization constant, it does not impact the binding surface as demonstrated by unchanged partner binding affinities. However, the CTE (only 4 residues in HP1a as compared with 87 residues in HP1b) is critical; the charged residues in HP1a are necessary for tight peptide binding. Examining a panel of amino acid substitutions in the HP1a CSD, we find that Leu-165 in HP1a interacts with HP2 but not PIWI, supporting the conclusion that different sites in the binding surface provide discrimination for partner selection. Partner sequence is also critical for affinity, as the remaining difference in binding between HP2 and PIWI polypeptides is eliminated by swapping the PXVXL motifs between the two. Taken together, these studies indicate that the binding surface of the HP1a CSD plus its short CTE provide the needed discrimination among HP1a's partners, and that the CTE is important for differentiating the interactions of the Drosophila HP1 paralogs.
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