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A truncated 2--helix F-box present in poxvirus ankyrin repeat proteins is sufficient for binding the SCF1 ubiquitin ligase complex

University of Otago

¹ E-mail: andy.mercer{at}otago.ac.nz

Poxviruses encode a large family of ankyrin-repeat (ANK) proteins most of which contain an F-box-like motif necessary for the interaction of the ANK proteins with SCF1 (Skp1-Cullin1-F-box) complexes. The viral motif is generally truncated compared to the 3--helix cellular F-box. Cellular F-box -helixes 1-3 and regions C-terminal to it have been shown to contribute to Skp1 binding. We report that the poxvirus F-boxes generally contain only two -helixes, corresponding to cellular F-box -helixes 1 and 2. A third -helix was detected in some poxvirus F-boxes, but was not predicted to interact with Skp1. All but one of the poxvirus ANK/F-box proteins examined terminated directly after the F-box, excluding any contribution by C-terminal regions to the binding of Skp1. Here we show that despite this truncation, the F-box of a prototypical poxvirus ANK protein containing 2--helixes, is not only necessary but also sufficient for interaction with SCF1.

Received 3 December 2008; accepted 16 January 2009.

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