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The c134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1a to dephosphorylate the a subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase


The c134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1a to dephosphorylate the a subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase



Proceedings of the National Academy of Sciences of the United States of America 94: 3-8



ISSN/ISBN: 0027-8424

The mechanism by which the herpes simplex virus 1 protein c134.5 precludes a shutoff of protein synthesis was investigated. In infected cells, the double-stranded RNA-dependent protein kinase (PKR) is activated but phosphorylation of the a subunit of eukaryotic translation initiation factor 2 (eIF-2a) and protein synthesis shutoff are seen only with c134.5- mutants. c134.5 and MyD116, the murine growth arrest and DNA damage gene 34 (GADD34) protein, were shown to bind protein phosphatase 1a in vitro. Protein synthesis in infected cells required phosphatase activity. eIF-2a-P phosphatase activity was high in wild-type- or mock-infected cells and significantly reduced in cells infected with c134.5- mutants. These findings indicate that c134.5 allows continued protein synthesis in the presence of activated PKR by causing phosphatase to dephosphorylate eIF-2a. The GADD34 protein may act in a similar fashion.

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Accession: 010001219

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