Histone chaperone exploits intrinsic disorder to switch acetylation specificity

Abstract

Histone chaperones have been shown to control the activity and specificity of histone-modifying enzymes. Here the authors establish a structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4, finding that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain.