About: Host cell factor C1 is a research topic. Over the lifetime, 192 publications have been published within this topic receiving 13899 citations. The topic is also known as: CFF & HCF-1.
TL;DR: The biochemical purification of MLL is reported and it is demonstrated that it associates with a cohort of proteins shared with the yeast and human SET1 histone methyltransferase complexes, including a homolog of Ash2, another Trx-G group protein, and a potential mechanism for regulating its antagonistic transcriptional properties.
Abstract: MLL (for mixed-lineage leukemia) is a proto-oncogene that is mutated in a variety of human leukemias. Its product, a homolog of Drosophila melanogaster trithorax, displays intrinsic histone methyltransferase activity and functions genetically to maintain embryonic Hox gene expression. Here we report the biochemical purification of MLL and demonstrate that it associates with a cohort of proteins shared with the yeast and human SET1 histone methyltransferase complexes, including a homolog of Ash2, another Trx-G group protein. Two other members of the novel MLL complex identified here are host cell factor 1 (HCF-1), a transcriptional coregulator, and the related HCF-2, both of which specifically interact with a conserved binding motif in the MLLN (p300) subunit of MLL and provide a potential mechanism for regulating its antagonistic transcriptional properties. Menin, a product of the MEN1 tumor suppressor gene, is also a component of the 1-MDa MLL complex. Abrogation of menin expression phenocopies loss of MLL and reveals a critical role for menin in the maintenance of Hox gene expression. Oncogenic mutant forms of MLL retain an ability to interact with menin but not other identified complex components. These studies link the menin tumor suppressor protein with the MLL histone methyltransferase machinery, with implications for Hox gene expression in development and leukemia pathogenesis.
TL;DR: Oct-2 displays a unique phosphorylation pattern that is absent from molecules lacking one or the other activation domain, suggesting the activation domains have a role in inducing protein phosphorylated.
TL;DR: These studies link the H2B transcriptional machinery to cell cycle regulators, and possibly to cellular metabolic state (redox status), and set the stage for studies of the underlying mechanisms and the basis for coordinated histone gene expression and coupling to DNA replication.
TL;DR: Immediate early genes of herpes simplex viruses contain one or more copies of the conserved TAAT-GARAT DNA motif and a virus-encoded regulatory protein (Vmw65) is believed to stimulate transcription via this element, although the protein does not bind directly to DNA.
Abstract: Immediate early genes of herpes simplex viruses contain one or more copies of the conserved TAAT-GARAT (where R is purine) DNA motif. A virus-encoded regulatory protein (Vmw65) is believed to stimulate transcription via this element, although the protein does not bind directly to DNA. Overlapping the TAATGARAT element in many cases is an octamer sequence (ATGCAAAT) that is involved both in transcription by RNA polymerases II and III and in adenovirus DNA replication. So far at least two proteins (OTF-1 and OTF-2) have been identified that bind to the octamer. We show that both affinity-purified OTF-1 and OTF-2 bind to the TAATGARAT sequence and that Vmw65 induces the formation of an additional complex that involves OTF-1 and that is further retarded in a band-shift gel assay. Complementation experiments involving addition of purified OTF-1 to nuclear extracts that have been depleted of endogenous OTF-1 show that at least one other cellular factor(s) is required for complex formation. This cellular factor may be involved in recognition of the GARAT sequence.
TL;DR: The activities of Oct-1 and HCF-1 - two important regulators of cellular gene expression and proliferation - illuminate strategies by which HSV might coexist with its host.