Wysocka, J., Reilly, P. T., Herr, W. (June 2001) Loss of HCF-1-chromatin association precedes temperature-induced growth arrest of tsBN67 cells. Molecular and Cellular Biology, 21 (11). pp. 3820-3829. ISSN 0270-7306
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Abstract
Human HCF-1 is a large, highly conserved, and abundant nuclear protein that plays an important but unknown role in cell proliferation. It also plays a role in activation of herpes simplex virus immediate-early gene transcription by the viral regulatory protein VP16. A single proline-to-serine substitution in the HCF-1 VP16 interaction domain causes a temperature-induced arrest of cell proliferation in hamster tsBN67 cells and prevents transcriptional activation by VP16, We show here that HCF-1 is naturally bound to chromatin in uninfected tells through its VP16 interaction domain. HCF-1 is chromatin bound in tsBN67 cells at permissive temperature but dissociates from chromatin before tsBN67 cells stop proliferating at the nonpermissive temperature, suggesting that loss of HCF-1 chromatin association is the primary cause of the temperature-induced tsBN67 cell proliferation arrest. We propose that the role of HCF-1 in cell proliferation is to regulate gene transcription by associating with a multiplicity of DNA-bound transcription factors through its VP16 interaction domain.
Item Type: | Paper |
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Uncontrolled Keywords: | HERPES-SIMPLEX VIRUS AMINO-TERMINAL DOMAIN ACTIVATION DOMAIN REPRESSOR SIN3 HCF VP16 PROTEIN COMPLEX FAMILY LUMAN |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > Chromatin dynamics |
CSHL Authors: | |
Communities: | CSHL labs > Herr lab |
Depositing User: | Matt Covey |
Date: | June 2001 |
Date Deposited: | 15 Jan 2014 20:36 |
Last Modified: | 15 Jan 2014 20:36 |
PMCID: | PMC87041 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/29333 |
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