In this issue of Cell, English et al. (2006) 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.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)