Bovine papillomavirus replicative helicase E1 is a target of the ubiquitin ligase APC
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Updated: Aug 26, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
Published on: January 2, 2026
Francisca Mechali1, Chiung-Yueh Hsu, Anna Castro
1Centre de Recherches de Biochimie Macromoléculaire, CNRS FRE 2593, IFR 122, 34 293 Montpellier Cedex 5, France.
Abstract:
The papillomavirus E1 replicative helicase is essential for replication and maintenance of extrachromosomal viral genomes in infected cells. We previously found that the bovine papillomavirus E1 protein is a substrate of the ubiquitin-dependent proteolytic pathway. Here we show that E1 is targeted for degradation by the anaphase-promoting complex (APC). Inhibition of APC activity by the specific inhibitor Emi1 or point mutations in the D-box and KEN-box motifs of E1 stabilize the protein and increase viral DNA replication in both a cell-free system and in living cells. These findings involve APC as the ubiquitin ligase that controls E1 levels to maintain a constant low copy number of the viral genome during latent infection.
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