Repressive chromatin structures need to be unravelled to allow DNA-bin
ding proteins access to their target sequences. This de-repression con
stitutes an important point at which transcription and presumably othe
r nuclear processes can be regulated(1,2). Energy-consuming enzyme com
plexes that facilitate the interaction of transcription factors with c
hromatin by modifying nucleosome structure are involved in this regula
tion(3-5). One such factor, nucleosome-remodelling factor (NURF), has
been isolated from Drosophila embryo extracts(4,6,7), We have now iden
tified a chromatin-accessibility complex (CHRAC) which uses energy to
increase the general accessibility of DNA in chromatin. However, unlik
e other known chromatin remodelling factors, CHRAC can also function d
uring chromatin assembly: it uses ATP to convert irregular chromatin i
nto a regular array of nucleosomes with even spacing. CHRAC combines e
nzymes that modulate nucleosome structure and DNA topology. Using mass
spectrometry, we identified two of the five CHRAC subunits as the ATP
ase ISWI, which is also part of NURF6,8, and topoisomerase II, The pre
sence of ISWI in different contexts suggests that chromatin remodellin
g machines have a modular nature and that ISWI has a central role in d
ifferent chromatin remodelling reactions.