The E2 trans-activating protein of bovine papillomavirus type 1 (BPV1) is serine-phosphorylated in vivo

G. Meneguzzi, R. Lathe, M. P. Kieny, N. Vogt

Research output: Contribution to journalArticlepeer-review

Abstract

The E2 open reading of bovine papillomavirus 1 (BPV1) encoded both positive and negative transcriptional regulatory factors. The full-length E2 gene polypeptide is a strong transcriptional transactivator that acts on enhancers within the papillomavirus long control region (LCR), and two shorter E2 proteins function as transcription repressors. A vaccinia recombinant virus harboring the full length E2 coding sequence of BPV1 directs the synthesis of a 48 kD phosphoprotein with specific DNA binding activity. We show that in BPV1-transformed cells the full-length transactivator is a phosphoprotein, whereas truncated E2 proteins were not detectably phosphorylated.

Original languageEnglish
Pages (from-to)1285-1290
Number of pages6
JournalOncogene
Volume4
Issue number11
Publication statusPublished - 1989

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