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. 1999 Jun 4;274(23):16437-43.
doi: 10.1074/jbc.274.23.16437.

Analysis of functional domains of the host cell factor involved in VP16 complex formation

T A Hughes  1 , S La Boissière, P O'Hare
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Free article

Analysis of functional domains of the host cell factor involved in VP16 complex formation

T A Hughes et al. J Biol Chem. .
Free article

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.

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