Asf1, a loveseat for a histone couple.
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.
Bao
Yunhe
Y
Department of Carcinogenesis, Science Park Research Division, M.D. Anderson Cancer Center, Smithville, TX 78957, USA.
Shen
Xuetong
X
D018797:Cell Cycle Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002843:Chromatin / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
C109731:ASF1 protein, S cerevisiae; D018797:Cell Cycle Proteins; D002843:Chromatin; D006657:Histones; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins