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Molecular and Cellular Biology, May 2000, p. 3568-3575, Vol. 20, No. 10
Center for Cancer Research and Department of
Biology, Massachusetts Institute of Technology, Cambridge,
Massachusetts 02139
Host cell factor 1 (HCF-1; also called C1) is a 230-kDa protein
which is cleaved posttranslationally into separate but associated N-
and C-terminal polypeptides. These polypeptides are components of the
C1 complex, along with Oct-1 and the viral protein VP16. The C1 complex
is formed when herpes simplex virus (HSV) infects a cell and is
responsible for transcription of the HSV immediate-early genes. A
temperature-sensitive mutation in the N-terminal kelch domain of HCF-1
reversibly arrests cells in a G0-like state when grown at
the nonpermissive temperature, and the same domain interacts with VP16
in the formation of the C1 complex. The form of HCF-1 in primary
G0 cells was investigated by using peripheral blood mononucleocytes and serum-arrested human primary fibroblasts. A novel
50-kDa N-terminal fragment of HCF-1 encompassing the kelch domain was
identified in the cytoplasm of these cells. This fragment arises by
proteolysis of the full-length HCF-1 protein and is able to associate
with VP16.
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Copyright © 2000, American Society for Microbiology. All rights reserved.
A Novel 50-Kilodalton Fragment of Host Cell Factor 1 (C1) in
G0 Cells

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Corresponding author. Mailing address: Center for
Cancer Research and Department of Biology, Massachusetts Institute of
Technology, 77 Massachusetts Ave., Cambridge, MA 02139. Phone: (617)
253-6421. Fax: (617) 253-3867. E-mail: sharppa{at}mit.edu.
Present address: Cancer Center, Massachusetts General Hospital,
Boston, MA 02114.
Present address: Molecular Neurogenetics Unit, Massachusetts
General Hospital, Charlestown, MA 02129.
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