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Background  The human herpes simplex virus (HSV)  h ost  c ell  f actor HCF-1 is a transcriptional coregulator that associates with both histone methyl- and acetyltransferases, and a histone deacetylase and regulates cell proliferation and division. In HSV-infected cells, HCF-1 associates with the viral protein VP16 to promote formation of a multiprotein–DNA transcriptional activator complex. The ability of HCF proteins to stabilize this VP16-induced complex has been conserved in diverse animal species including  Drosophila melanogaster  and  Caenorhabditis elegans  suggesting that VP16 targets a conserved cellular function of HCF-1.    Methodology/Principal Findings  To investigate the role of HCF proteins in animal development, we have characterized the effects of loss of the HCF-1 homolog in  C. elegans , called Ce HCF-1. Two large  hcf-1  deletion mutants ( pk924  and  ok559 ) are viable but display reduced fertility. Loss of Ce HCF-1 protein at reduced temperatures (e.g., 12°C), however, leads to a high incidence of embryonic lethality and early embryonic mitotic and cytokinetic defects reminiscent of mammalian cell-division defects upon loss of HCF-1 function. Even when viable, however, at normal temperature, mutant embryos display reduced levels of phospho-histone H3 serine 10 (H3S10P), a modification implicated in both transcriptional and mitotic regulation. Mammalian cells with defective HCF-1 also display defects in mitotic H3S10P status.    Conclusions/Significance  These results suggest that HCF-1 proteins possess conserved roles in the regulation of cell division and mitotic histone phosphorylation.

Epigenetic Regulation of Histone H3 Serine 10 Phosphorylation Status by HCF-1 Proteins in C. elegans and Mammalian Cells