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J Biol Chem, Vol. 275, Issue 20, 14787-14790, May 19, 2000

ACCELERATED PUBLICATION
Purification and Characterization of a Human Factor That Assembles and Remodels Chromatin^*

Gary LeRoy, Alejandra Loyola, William S. Lane^§, and Danny Reinberg^¶

From the  Howard Hughes Medical Institute, Division of Nucleic Acid Enzymology, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854 and the ^§ Harvard Microchemistry Facility, Harvard University, Cambridge, Massachusetts 02138

We have previously reported the isolation and characterization of a nucleosome remodeling and spacing factor, RSF. One of the RSF subunits is hSNF2h, a SNF2 homologue. Here we set out to isolate and characterize other hSNF2h-containing complexes. We have identified a novel hSNF2h complex that facilitates ATP-dependent chromatin assembly with the histone chaperone NAP-1. The complex possesses ATPase activity that is DNA-dependent and nucleosome-stimulated. This complex is capable of facilitating ATP-dependent nucleosome remodeling and transcription initiation from chromatin templates. In addition to hSNF2h, this complex also contains a 190-kDa protein encoded by the BAZ1A gene. Since both subunits are homologues of the Drosophila ACF complex (ATP-utilizing chromatin assembly and remodeling factor), we have named this factor human ACF or hACF.

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