Structural Insight into Coordinated Recognition of Trimethylated Histone H3 Lysine 9 (H3K9me3) by the Plant Homeodomain (PHD) and Tandem Tudor Domain (TTD) of UHRF1 (Ubiquitin-like, Containing PHD and RING Finger Domains, 1) Protein*
Cheng J, Yang Y, Fang J, Xiao J, Zhu T, Chen F, Wang P, Li Z, Yang H, Xu Y. Structural Insight into Coordinated Recognition of Trimethylated Histone H3 Lysine 9 (H3K9me3) by the Plant Homeodomain (PHD) and Tandem Tudor Domain (TTD) of UHRF1 (Ubiquitin-like, Containing PHD and RING Finger Domains, 1) Protein*. Journal Of Biological Chemistry 2012, 288: 1329-1339. PMID: 23161542, PMCID: PMC3543016, DOI: 10.1074/jbc.m112.415398.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCCAAT-Enhancer-Binding ProteinsCrystallizationFluorescence Resonance Energy TransferHistonesHumansLysineMethylationProtein ConformationRING Finger DomainsUbiquitin-Protein LigasesUbiquitinationConceptsTandem Tudor domainHistone H3 lysine 9Plant homeodomainH3 lysine 9Tudor domainHistone methylationLysine 9DNA methylationStructural insightsDNA replication forksCoordinated recognitionImportant epigenetic regulatorsUnmodified histone H3Unmodified H3UHRF1 proteinReplication forksHistone H3Epigenetic regulatorsLys-9Autoubiquitination activityLys-4H3K9me3UHRF1Linker regionBiochemical experiments