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J Gen Virol 78 (1997), 171-177
© 1997 Society for General Microbiology
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Journal of General Virology, Vol 78, 171-177, Copyright © 1997 by Society for General Microbiology

ARTICLES

Casein kinase II phosphorylates bovine papillomavirus type 1 E1 in vitro at a conserved motif

GD McShan and VG Wilson
Department of Medical Microbiology and Immunology, Texas A&M University Health Science Center, College Station 77843-1114, USA.

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 El protein has been shown to be multiply phosphorylated in vivo, 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 in vitro substrate for CKII at the serine within this conserved motif.


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