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. 1989 Oct 19;341(6243):624-30.
doi: 10.1038/341624a0.

The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16

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The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16

S Stern et al. Nature. .

Abstract

The herpes simplex virus transactivator VP16 participates in the formation of a multiprotein-DNA complex with the ubiquitous octamer-motif-binding factor Oct-1. Complex formation is dependent on specific amino acids in the Oct-1 homoeodomain which are in positions analogous to positive control mutations in helix 2 of the lambda phage repressor helix-turn-helix motif, indicating that this structure is an ancient target for protein-protein interactions mediating transcriptional control.

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