SUMO-1 Modification of Bovine Papillomavirus E1 Protein Is Required for Intranuclear Accumulation

作者：Dhandapani Rangasamy, Kelly Woytek, Saleem Ahmad Khan, Van G. Wilson · 发表于：Journal of Biological Chemistry · 年份：2000 · DOI：10.1074/jbc.m007777200 · 被引用次数：83 · 研究领域：Ubiquitin and proteasome pathways、T-cell and Retrovirus Studies、Virus-based gene therapy research

The E1 protein is a multifunctional, origin-binding helicase that is essential for replication of papillomaviruses. Recently, bovine papillomavirus E1 was shown to be post-translationally modified by the addition of the SUMO-1 polypeptide. Here we show that the site of sumoylation maps to lysine residue 514. This lysine and the flanking sequences are well conserved in human papillomavirus (HPV) E1 proteins. Both HPV1a and HPV18 E1 proteins are substrates for sumoylation in vitro, which is consistent with this modification being a general property of E1 proteins. Mutations, which impair the sumoylation of bovine papillomavirus E1, prevent normal nuclear accumulation of E1 with a concomitant loss of replication capacity. These results suggest that sumoylation plays a role in nuclear transport and could regulate the E1 replication function by controlling access to the nuclear replication domains.