Structural basis of Eco1-mediated cohesin acetylationMore about Open Access at the Crick
Authors listWilliam CH Chao Benjamin O Wade Celine Bouchoux Andrew Jones Andrew G Purkiss Stefania Federico Nicola O'Reilly Bram Snijders Frank Uhlmann Martin R Singleton
Sister-chromatid cohesion is established by Eco1-mediated acetylation on two conserved tandem lysines in the cohesin Smc3 subunit. However, the molecular basis of Eco1 substrate recognition and acetylation in cohesion is not fully understood. Here, we discover and rationalize the substrate specificity of Eco1 using mass spectrometry coupled with in-vitro acetylation assays and crystallography. Our structures of the X. laevis Eco2 (xEco2) bound to its primary and secondary Smc3 substrates demonstrate the plasticity of the substrate-binding site, which confers substrate specificity by concerted conformational changes of the central β hairpin and the C-terminal extension.
Journal Scientific Reports