Abstract
Structural Biology The yeast SWR1 complex, a member of the INO80 family of nucleosome remodelers, exchanges the H2A-H2B histone dimer for the Htz1 variant–containing dimer. Unlike all other remodelers, SWR1 does not translocate the nucleosome. Willhoft et al. applied structural and single-molecule analyses to show that the interaction between SWR1 and the nucleosome destabilizes the DNA wrapped around the histone core. This SWR1-catalyzed partial unwrapping of the DNA was regulated by adenosine triphosphate (ATP) binding but did not require ATP hydrolysis. Science , this issue p. [eaat7716][1] [1]: /lookup/doi/10.1126/science.aat7716
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