Structure of the UHRF1 Tandem Tudor Domain Bound to a Methylated Non-histone Protein, LIG1, Reveals Rules for Binding and Regulation

International audienceGraphical Abstract Highlights d The crystal structure of UHRF1 TTD domain bound to the LIG1K126me3 was determined d Arg121 of LIG1 is a key residue for high-affinity binding to the TTD d Phosphorylation of LIG1T123 negatively regulates the interaction with UHRF1 d LIG1K126me3 binding changes UHRF1 structure from closed to open Correspondence pierre-antoine.defossez@ univ-paris-diderot.fr (P.-A.D.), [email protected] (K.A.) In Brief The interaction between UHRF1 and LIG1K126me3 is essential for DNA methylation maintenance. Kori et al. determined the crystal structure of the UHRF1 TTD bound to a LIG1K126me3 peptide, revealing the basis for the high TTD-binding affinity of LIG1K126me3, regulation by phosphorylation, and that LIG1K126me3 binding switches the overall structure of UHRF1