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Vol. 273, Issue 3, 1435-1443, January 16, 1998

The R1 Subunit of Herpes Simplex Virus Ribonucleotide Reductase Is a Good Substrate for Host Cell Protein Kinases but Is Not Itself a Protein Kinase

Yves Langelier, Louise Champoux, Martine Hamel^¶, Claire Guilbault, Nathalie Lamarche, Pierrette Gaudreau, and Bernard Massie^¶

From the  Institut du Cancer de Montréal and  Centre de Recherche du Centre Hospitalier de l'Université de Montréal, Pavillon Notre-Dame, 1560 est, Sherbrooke, Montréal, Québec H2L 4M1, Canada, and the ^¶ Institut de Recherche en Biotechnologie, 6100 avenue Mont-Royal, Montréal, Québec H4P 2R2, Canada

The N terminus of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is believed to be a protein kinase domain mainly because the R1 protein was phosphorylated in a protein kinase assay on blot. Using Escherichia coli and adenovirus expression vectors to produce R1, we found that, whereas the reductase activity of both recombinant proteins was similar, efficient phosphorylation of R1 and casein in the presence of Mg²⁺ was obtained only with the R1 purified from eukaryotic cells. Phosphorylation of this R1, in solution or on blot, results mainly from the activity of casein kinase II (CKII), a co-purifying protein kinase. Labeling on blot occurs from CKII leakage off the membrane and its subsequent high affinity binding to in vivo CKII-phosphorylated R1. CKII target sites were mapped to an acidic serine-rich segment of the R1 N terminus. Improvement in purification of the R1 expressed in eukaryotic cells nearly completely abolished its phosphorylation potential. An extremely low level of phosphorylation observed in the presence of Mn²⁺ with the R1 produced in E. coli was probably due to an unidentified prokaryotic protein kinase. These results provide evidence that the herpes simplex virus type 2 R1 does not possess an intrinsic protein kinase activity.

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