Chromatin remodelers are ATP-dependent machines responsible for directionally 
shifting nucleosomes along DNA. We are interested in defining which elements of 
the chromodomain helicase DNA-binding protein 1 (Chd1) remodeler are necessary 
and sufficient for sliding nucleosomes. This work focuses on the polypeptide 
segment that joins the ATPase motor to the C-terminal DNA-binding domain. We 
identify amino acid positions outside the ATPase motor that, when altered, 
dramatically reduce nucleosome sliding ability and yet have only ∼3-fold 
reduction in ATPase stimulation by nucleosomes. These residues therefore appear 
to play a role in functionally coupling ATP hydrolysis to nucleosome sliding, 
and suggest that the ATPase motor requires cooperation with external elements to 
slide DNA past the histone core.