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HP1 proteins compact DNA into mechanically and positionally stable phase separated domains
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HP1 proteins compact DNA into mechanically and positionally stable phase separated domains
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Journal Article
HP1 proteins compact DNA into mechanically and positionally stable phase separated domains
2021
Overview
In mammals, HP1-mediated heterochromatin forms positionally and mechanically stable genomic domains even though the component HP1 paralogs, HP1α, HP1β, and HP1γ, display rapid on-off dynamics. Here, we investigate whether phase-separation by HP1 proteins can explain these biological observations. Using bulk and single-molecule methods, we show that, within phase-separated HP1α-DNA condensates, HP1α acts as a dynamic liquid, while compacted DNA molecules are constrained in local territories. These condensates are resistant to large forces yet can be readily dissolved by HP1β. Finally, we find that differences in each HP1 paralog’s DNA compaction and phase-separation properties arise from their respective disordered regions. Our findings suggest a generalizable model for genome organization in which a pool of weakly bound proteins collectively capitalize on the polymer properties of DNA to produce self-organizing domains that are simultaneously resistant to large forces at the mesoscale and susceptible to competition at the molecular scale.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
Biochemistry and Chemical Biology
/ Chromobox Protein Homolog 5 - genetics
/ Chromobox Protein Homolog 5 - metabolism
/ Chromosomal Proteins, Non-Histone - genetics
/ Chromosomal Proteins, Non-Histone - metabolism
/ DNA
/ Genomes
/ Genomics
/ Heterochromatin - metabolism
/ Humans
/ Polymers
/ Proteins
