1887

Abstract

The E1 protein of bovine papillomavirus type 1 (BPV-1) is a phosphoprotein which specifically binds and unwinds the virus replication origin by ATP- dependent helicase activity. The E1 protein has been shown to be multiply phosphorylated , although the sites of modification are incompletely mapped. Examination of the predicted amino acid sequence of all available E1 proteins revealed strong conservation between amino acids 25 and 60 of a motif consisting of a serine residue followed by a stretch of acidic residues. This conserved motif resembled a phosphorylation consensus site for the ubiquitous cellular kinase casein kinase II (CKII). Biochemical and mutational analysis demonstrated that the BPV-1 E1 protein is an substrate for CKII at the serine within this conserved motif.

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1997-01-01
2023-01-28
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