ArticleCell reports methods2025
Understanding how genetically encoded tags and crowding agents affect phase separation by heterochromatin protein HP1α.
Article in Cell reports methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Article
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- Preferential formation of NUP98-KDM5A condensates at specific H3K4me3-rich loci drives leukemogenic gene expression.bioRxiv : the preprint server for biology · 2026Article
- Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro.EMBO reports · 2026Article
- The dark side of fluorescent protein tagging-the impact of protein tags on biomolecular condensation.Molecular biology of the cell · 2025Article
- Fluorescent protein tags affect the condensation properties of a phase-separating viral protein.Molecular biology of the cell · 2024Article
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Abstract
The heterochromatin protein HP1α (heterochromatin protein 1 alpha) phase separates in vitro and displays properties compatible with phase separation in cells. Phase separation of HP1α in cells is typically studied using genetically encoded fluorescent tags such as green fluorescent protein (GFP). Whether such tags affect the intrinsic phase separation properties of HP1α is understudied. We assessed how tag size and linker length affect phase separation by HP1α in vitro. GFP tags inhibited phase separation by HP1α. In contrast, an UnaG tag with a 16 amino acid glycine-glycine-serine (GGS) linker minimally perturbed HP1α phase separation in vitro and could be used to visualize HP1α dynamics in cells. We further investigated the effects of a commonly used crowding agent, polyethylene glycol (PEG). PEG induced phase separation of proteins with no propensity to phase separate under physiological buffer conditions and dampened the effects of HP1α mutations. Therefore, phase separation of biological macromolecules with PEG-containing crowding agents should be interpreted with caution.
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