De. Kelley et al., CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin, CHROMOSOMA, 108(1), 1999, pp. 10-25
CHD1, an M-r similar to 200,000 protein that contains a chromodomain (C), a
n ATPase/helicase-like domain (H) and a DNA-binding domain (D), was previou
sly shown to be associated with decompacted interphase chromatin in mammali
an cells and with transcriptionally active puffs and interbands in Drosophi
la polytene chromosomes. We now show by transient transfection experiments
with genes expressing wild-type and mutant forms of CHD1 that both the C an
d H domains are essential for its proper association with chromatin. We als
o present evidence for an in vivo interaction between CHD1 and a novel HMG
box-containing protein, SSRP1, which involves an amino-terminal segment of
CHD1 that does not include the chromodomain. Immunocytochemical analyses in
dicated that CHD1 and SSRP1 colocalize in both mammalian nuclei and Drosoph
ila polytene chromosomes.