Journal
MOLECULAR CELL
Volume 54, Issue 5, Pages 879-886Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2014.04.003
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Funding
- Chinese Ministry of Science and Technology [2010CB944903, 2012CB910702]
- Natural Science Foundation of China [91219307, 31210103914]
- Strategic Priority Research Program [XDB08010100]
- Chinese Academy of Sciences [KJZD-EW-L05]
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Methylated cytosine of CpG dinucleotides in vertebrates may be oxidized by Tet proteins, a process that can lead to DNA demethylation. The predominant oxidation product, 5-hydroxymethylcytosine (5hmC), has been implicated in embryogenesis, cell differentiation, and human diseases. Recently, the SRA domain of UHRF2 (UHRF2-SRA) has been reported to specifically recognize 5hmC, but how UHRF2 recognizes this modification is unclear. Here we report the structure of UHRF2-SRA in complex with a 5hmC-containing DNA. The structure reveals that the conformation of a phenylalanine allows the formation of an optimal 5hmC binding pocket, and a hydrogen bond between the hydroxyl group of 5hmC and UHRF2-SRA is critical for their preferential binding. Further structural and biochemical analyses unveiled the role of SRA domains as a versatile reader of modified DNA, and the knowledge should facilitate further understanding of the biological function of UHRF2 and the comprehension of DNA hydroxymethylation in general.
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