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What's up in Epigenetics & Proteomics #1


Research paper highlight

The mechanism for regulation of H3K9me3 and hm-DNA recognition by URHF1 revealed
UHRF1 (Ubiquitin-like containing PHD and RING Finger domains 1) is an epigenetic integrator that functions as a hub protein able to read epigenetics marks and to recruit the corresponding writers that catalyse these marks. Furthermore, UHRF1 ensures the link between H3K9me3 and DNA methylation maintenance. How this link is operating is still elusive.

However, in a recent paper published in Nature Communications, Fang et al. found that both the tandem Tudor domain (TTD) and the plant homeodomain (PHD) are regulated by hemimethylated-DNA to recognize histone H3K9me3. The closed form of UHRF1 is unable to bind H3K9me3 but when its SRA-spacer domain interacts with hemi-methylated DNA, UHRF1 adopts an open conformational state that releases the TTD-PHD tandem to freely interact with H3K9me3.

The authors suggested that when the SRA–Spacer dissociates from hemimethylated-DNA and binds to DNMT1, UHRF1 may keep the complex associated with chromatin through the interaction between TTD–PHD and H3K9me3. This allows DNMT1 to subsequently target proper DNA substrate for methylation. The study highlights the importance of the role of the different domains of UHRF1 and sheds new light on the usefulness to link H3K9me3 and DNA methylation.

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