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Molecular and Cellular Biology, September 2000, p. 6721-6730, Vol. 20, No. 18
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

HCF-1 Amino- and Carboxy-Terminal Subunit Association through Two Separate Sets of Interaction Modules: Involvement of Fibronectin Type 3 Repeats

Angus C. Wilson,1,2 Michael Boutros,1,dagger Kristina M. Johnson,2,Dagger and Winship Herr1,*

Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724,1 and Department of Microbiology and Kaplan Cancer Center, New York University School of Medicine, New York, New York 100162

Received 6 March 2000/Returned for modification 9 April 2000/Accepted 9 June 2000

When herpes simplex virus infects permissive cells, the viral regulatory protein VP16 forms a specific complex with HCF-1, a preexisting nuclear protein involved in cell proliferation. The majority of HCF-1 in the cell is a complex of associated amino (HCF-1N)- and carboxy (HCF-1C)-terminal subunits that result from an unusual proteolytic processing of a large precursor polypeptide. Here, we have characterized the structure and function of sequences required for HCF-1N and HCF-1C subunit association. HCF-1 contains two matched pairs of self-association sequences called SAS1 and SAS2. One of these matched association sequences, SAS1, consists of a short 43-amino-acid region of the HCF-1N subunit, which associates with a carboxy-terminal region of the HCF-1C subunit that is composed of a tandem pair of fibronectin type 3 repeats, a structural motif known to promote protein-protein interactions. Unexpectedly, the related protein HCF-2, which is not proteolyzed, also contains a functional SAS1 association element, suggesting that this element does not function solely to maintain HCF-1N and HCF-1C subunit association. HCF-1N subunits do not possess a nuclear localization signal. We show that, owing to a carboxy-terminal HCF-1 nuclear localization signal, HCF-1C subunits can recruit HCF-1N subunits to the nucleus.

* Corresponding author. Mailing address: Cold Spring Harbor Laboratory, P.O. Box 100, Cold Spring Harbor, NY 11724. Phone: (516) 367-8401. Fax: (516) 367-8454. E-mail: herr{at}cshl.org.

dagger Present address: Department of Genetics, Harvard Medical School, Boston, MA 02115.

Dagger Present address: Department of Biological Chemistry, University of California, Los Angeles, School of Medicine, Los Angeles, CA 90095.

Molecular and Cellular Biology, September 2000, p. 6721-6730, Vol. 20, No. 18
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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