Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-04-05

AUTHORS

Jian Fang, Jingdong Cheng, Jiaolong Wang, Qiao Zhang, Mengjie Liu, Rui Gong, Ping Wang, Xiaodan Zhang, Yangyang Feng, Wenxian Lan, Zhou Gong, Chun Tang, Jiemin Wong, Huirong Yang, Chunyang Cao, Yanhui Xu

ABSTRACT

UHRF1 is an important epigenetic regulator for maintenance DNA methylation. UHRF1 recognizes hemi-methylated DNA (hm-DNA) and trimethylation of histone H3K9 (H3K9me3), but the regulatory mechanism remains unknown. Here we show that UHRF1 adopts a closed conformation, in which a C-terminal region (Spacer) binds to the tandem Tudor domain (TTD) and inhibits H3K9me3 recognition, whereas the SET-and-RING-associated (SRA) domain binds to the plant homeodomain (PHD) and inhibits H3R2 recognition. Hm-DNA impairs the intramolecular interactions and promotes H3K9me3 recognition by TTD-PHD. The Spacer also facilitates UHRF1-DNMT1 interaction and enhances hm-DNA-binding affinity of the SRA. When TTD-PHD binds to H3K9me3, SRA-Spacer may exist in a dynamic equilibrium: either recognizes hm-DNA or recruits DNMT1 to chromatin. Our study reveals the mechanism for regulation of H3K9me3 and hm-DNA recognition by URHF1. More... »

PAGES

11197

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms11197

DOI

http://dx.doi.org/10.1038/ncomms11197

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038789614

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27045799


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