The E2 trans-activating protein of bovine papillomavirus type 1 (BPV1) is serine-phosphorylated in vivo.
The E2 open reading frame of bovine papillomavirus 1 (BPV1) encodes 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.
Meneguzzi
G
G
U273-INSERM, Centre de Biochimie, Parc Valrose, Nice, France.
Lathe
R
R
Kieny
M P
MP
Vogt
N
N
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001483:Base Sequence; D052688:Bovine papillomavirus 1 / Q000235:genetics* / Q000378:metabolism; D002460:Cell Line; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004279:DNA, Viral / Q000235:genetics / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D015870:Gene Expression; D005814:Genes, Viral; D008969:Molecular Sequence Data; D027383:Papillomaviridae / Q000235:genetics*; D010750:Phosphoproteins / Q000032:analysis / Q000096:biosynthesis; D015183:Restriction Mapping; D015534:Trans-Activators / Q000235:genetics* / Q000378:metabolism
D000596:Amino Acids; D004279:DNA, Viral; D010750:Phosphoproteins; D015534:Trans-Activators