title: Analysis of functional domains of the host cell factor involved in VP16 complex formation.
abstract: We present biochemical analyses of the regions of the host cell factor (HCF) involved in VP16 complex formation and in the association between the N- and C-terminal domains of HCF itself. We show that the kelch repeat region of HCF (residues 1-380) is sufficient for VP16 complex formation, but that residues C-terminal to the repeats (positions 381-450) interfere with this activity. However, these latter residues are required for the interaction between the N- and C-terminal regions of HCF. The extreme C-terminal region of HCF, corresponding to an area of strong conservation with a Caenorhabditis elegans homologue, is sufficient for interaction with the N-terminal region. These results are discussed with respect to possible differences in the roles of HCF in VP16 activity versus its normal cellular function.
authors.affiliation: Marie Curie Research Institute, The Chart, Oxted, Surrey, RH8 0TL, United Kingdom.
authors.forename: T A
authors.initials: TA
authors.lastname: Hughes
authors.forename: S
authors.initials: S
authors.lastname: La Boissière
authors.forename: P
authors.initials: P
authors.lastname: O'Hare
mesh_terms: D000818:Animals; D001665:Binding Sites; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins; D017405:Herpes Simplex Virus Protein Vmw65 / Q000378:metabolism*; D051863:Host Cell Factor C1; D006801:Humans; D046911:Macromolecular Substances; D011506:Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014157:Transcription Factors
chemical_list: D029742:Caenorhabditis elegans Proteins; C497692:HCFC1 protein, human; D017405:Herpes Simplex Virus Protein Vmw65; D051863:Host Cell Factor C1; D046911:Macromolecular Substances; D011506:Proteins; D014157:Transcription Factors; C497691:hcf-1 protein, C elegans