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| What's
up in Epigenetics & Proteomics #1 |
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Research
paper highlight
The
mechanism for
regulation of H3K9me3 and hm-DNA recognition by URHF1 revealed |
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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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