Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 21, Issue 11, Pages 3820-3829Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.21.11.3820-3829.2001
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Funding
- NCI NIH HHS [CA13106, P01 CA013106] Funding Source: Medline
- NIGMS NIH HHS [GM54598, R01 GM054598] Funding Source: Medline
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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.
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