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

Virus Research Unit, Department of Microbiology and Immunology, University of Otago, PO Box 56, Dunedin 9016, New Zealand

Correspondence
Andrew A. Mercer
andy.mercer{at}stonebow.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 with the three--helix cellular F-box. Cellular F-box -helices 1–3 and regions C-terminal to them have been shown to contribute to Skp1 binding. We report that the poxvirus F-boxes generally contain only two -helices, corresponding to cellular F-box -helices 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 two -helices, is not only necessary but also sufficient for interaction with SCF1.

A supplementary figure showing -helix predictions of poxvirus F-boxes generated by structure modelling is available with the online version of this paper.

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