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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 LangelierDagger , Louise ChampouxDagger , Martine Hamel, Claire GuilbaultDagger , Nathalie LamarcheDagger , Pierrette Gaudreau, and Bernard Massie

From the Dagger  Institut du Cancer de Montréal and Dagger Dagger  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.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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