Eukaryotic DNA replication is initiated at multiple chromosomal locations that are targeted by the origin recognition complex (ORC), a conserved protein machine containing multiple ATPase sites. In budding yeast, ORC binds to specific DNA sequences known as autonomously replicating sequences (ARSs) that are mostly nucleosome depleted. However, nucleosomes may still inhibit the licensing of some origins by occluding ORC binding and subsequent MCM helicase loading. In collaboration with the O’Donnell Lab and the Bai Lab, we use a combination of single-molecule, biochemical, and genomic approaches to show that ORC can eject histones from a nucleosome in an ATP-dependent manner. ORC selectively evicts H2A-H2B dimers but leaves the (H3-H4)2 tetramer on DNA. It also discriminates canonical H2A from the H2A.Z variant, evicting the former while retaining the latter. The bromo-adjacent homology domain of the Orc1 subunit is essential for the histone removal activity. These findings suggest that ORC is a bona fide nucleosome remodeler that helps to sculpt a local chromatin environment optimal for origin activity.