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J Biol Chem, Vol. 273, Issue 33, 20737-20743, August 14, 1998

The ₁34.5 Protein of Herpes Simplex Virus 1 Has the Structural and Functional Attributes of a Protein Phosphatase 1 Regulatory Subunit and Is Present in a High Molecular Weight Complex with the Enzyme in Infected Cells

Bin He, Martin Gross^§, and Bernard Roizman

From the  Marjorie B. Kovler Viral Oncology Laboratories and the ^§ Department of Pathology, The University of Chicago, Chicago, Illinois 60637

The carboxyl-terminal domain of the ₁34.5 protein of the herpes simplex virus 1 binds to protein phosphatase 1 (PP1) and is required to prevent the shut-off of protein synthesis resulting from phosphorylation of the  subunit of eIF-2 by the double-stranded RNA-activated protein kinase. The corresponding domain of the conserved GADD34 protein homologous to ₁34.5 functionally substitutes for ₁34.5. This report shows that ₁34.5 and PP1 form a complex in the infected cells, that fractions containing this complex specifically dephosphorylate eIF-2, and that both ₁34.5 and GADD34 proteins contain the amino acid sequence motif common to subunits of PP1 that is required for binding to the PP1 catalytic subunit. An oligopeptide containing this motif competes with ₁34.5 for binding to PP1. Substitution of Val¹⁹³ and Phe¹⁹⁵ in the PP1-binding motif abolished activity. These results suggest that the carboxyl-terminal domain of ₁34.5 protein has the structural and functional attributes of a subunit of PP1 specific for eIF-2, that it has evolved to preclude shut-off of protein synthesis, and that GADD34 may have a similar function.

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