Histone acetylation sites reshape DNA condensates, revealing a potential gene-control mechanism
A research team from AIST, the Institute of Science Tokyo, and Ritsumeikan University has demonstrated that the phase behavior of histone–DNA condensates depends on the site of histone acetylation.
Researchers from AIST, Tokyo Institute of Science, and Ritsumeikan University have uncovered a new role for histone acetylation in shaping DNA condensates, potentially offering a fresh perspective on gene regulation. Histone acetylation, a key post-translational modification, has been linked to both cancer and neurodegenerative diseases, while liquid-liquid phase separation (LLPS)—a process where proteins and DNA assemble into droplet-like structures—has also been identified as a critical factor in gene regulation.
Despite their importance, the connection between histone modifications and LLPS has remained elusive. The study, published in the Journal of the American Chemical Society, reveals that the location of histone H3 acetylation sites significantly impacts the condensation of histone H3 and DNA molecules. This site-specific control of condensate formation suggests that histone modifications not only influence whether phase separation occurs but also dictate how DNA is organized within the cell.
Such insights could lead to novel therapeutic strategies for diseases characterized by aberrant gene expression, highlighting the potential of targeting epigenetic mechanisms like histone acetylation.
Written by urgent.news from Phys.org's reporting — not their text. Machine-written — may contain errors; check the original before relying on it.
