| Literature DB >> 17081967 |
Abstract
In this issue of Cell, English et al. present the first crystal structure of a histone chaperone (Asf1) bound to histones (the H3/H4 heterodimer). The structure provides insights into how histone chaperones participate in nucleosome disassembly. It reveals that Asf1 physically blocks (H3/H4)(2) tetramer formation and that the C terminus of H4 undergoes a dramatic conformational change upon binding to Asf1.Mesh：
Substances：
Year: 2006 PMID： 17081967 DOI： 10.1016/j.cell.2006.10.021
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582