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Molecular and Cellular Biology, October 2003, p. 6759-6768, Vol. 23, No. 19
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.19.6759-6768.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Functional Analysis of the Subunits of the Chromatin Assembly Factor RSF

Alejandra Loyola,1,2,{dagger} Jing-Yi Huang,3 Gary LeRoy,1,2 Sherrie Hu,1,2 Yuh-Hwa Wang,2 Robert J. Donnelly,4,{dagger} William S. Lane,5 Sheng-Chung Lee,3 and Danny Reinberg1,2*

Howard Hughes Medical Institute,2 Division of Nucleic Acids Enzymology,4 Department of Biochemistry, University of Medicine and Dentistry of New JerseyRobert Wood Johnson Medical School, Piscataway, New Jersey 08854,3 Institute of Molecular Medicine, National Taiwan University, Taipei, Taiwan,5 Molecular Resource Facility, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark, New Jersey 07103,1 Microchemistry and Proteomics Analysis Facility, Harvard University, Cambridge, Massachusetts 021386

Received 17 April 2003/ Returned for modification 15 May 2003/ Accepted 17 June 2003

The human ISWI-containing factor RSF (for remodeling and spacing factor) is composed of two subunits: the ATPase hSNF2H and p325 (Rsf-1), a protein encoded by a novel human gene. We previously showed that RSF mediates nucleosome deposition and generates regularly spaced nucleosome arrays. Here we report the characterization of the largest subunit of RSF, Rsf-1. We found that Rsf-1 is a highly acidic protein containing a plant homology domain. The present study includes the cloning of Rsf-1, the preparation of recombinant RSF, and the dissection of the role of each subunit in the chromatin assembly reaction. The sequence of the gene for Rsf-1 includes a recently characterized cDNA, HBXAP; postulated to be involved in the transcriptional regulation of the hepatitis B virus. HBXAP actually contains a 252-amino-acid truncation of the amino terminus of Rsf-1. Finally, comparison of HBXAP and Rsf-1 properties shows that they are functionally different.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, University of Medicine and Dentistry of New Jersey and Robert Wood Johnson Medical School, Piscataway, NJ 08854. Phone: (732) 235-4195. Fax: (732) 235-5294. E-mail: reinbedf{at}umdnj.edu.

{dagger} Present address: Institut Curie, Section de Recherche, UMR218, 75231 Paris Cedex 05, France.

Molecular and Cellular Biology, October 2003, p. 6759-6768, Vol. 23, No. 19
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.19.6759-6768.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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