抄録
We have solved the crystal structures of the yeast chromatin remodeling factor ISW1a (ΔATPase) complex with and without bound duplex DNA at resolutions of 3.60 and 3.25 Å, respectively. The DNA-bound form reveals the characteristic feature of each protein component of ISW1a (HSS and Ioc3) individually gripping a DNA molecule. In addition to these X-ray structures, we have performed Cryo-EM analyses of ISW1a-nucleosome complex, and a biochemical analysis of the remodeling action of ISW1a using a di-nucleosome as substrate. Based on the composite analysis we can elucidate the remodeling mechanism of ISW1a for two nucleosomes in atomic detail.
