Asf1, a loveseat for a histone couple.
basic_science · Level V
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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.
Medical subject headings
- Cell Cycle Proteins
- Histones
- Molecular Chaperones
- Saccharomyces cerevisiae Proteins