2015 年 57 巻 1 号 p. 53-58
DNA methylation and histone modifications are major epigenetic traits for regulating the various chromatin template processes in mammals. UHRF1, together with Dnmt1, is an essential factor for maintenance of DNA methylation in somatic cells. UHRF1 has five functional domains, namely UBL, tandem tudor domain (TTD), PHD finger, SRA domain and RING finger. UHRF1 has been shown to bind to histone H3 containing tri-methylated K9 (H3K9me3), but the molecular mechanism of histone H3 recognition by UHRF1 TTD-PHD domain is unclear. Here, I report the structural study of UHRF1 TTD-PHD domain, which reveals how UHRF1 recognizes multiple histone modifications on histone H3 tail.combination of X-ray crystallography, NMR and small-angle X-ray scattering reveal the higher order structure formation of UHRF1 TTD-PHD domain, structural induction of histone H3 tail and the importance of linker between TTD and PHD finger.