Disruption of cellular translational control by a viral truncated eukaryotic translation initiation factor 2α kinase homolog

Thomas E. Dever, Rajaraman Sripriya, Jeanne R. Mclachlin, Jingfang Lu, John R. Fabian, Scot R. Kimball, Lois K. Miller

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

Phosphorylation of eukaryotic translation initiation factor 2α (eIF2a) is a common cellular mechanism to limit protein synthesis in stress conditions. Baculovirus PK2, which resembles the C-terminal half of a protein kinase domain, was found to inhibit both human and yeast eIF2α kinases. Insect cells infected with wild-type, but not pk2-deleted, baculovirus exhibited reduced eIF2α phosphorylation and increased translational activity. The negative regulatory effect of human protein kinase RNA- regulated (PKR), an eIF2α kinase, on virus production was counteracted by PK2, indicating that baculoviruses have evolved a unique strategy for disrupting a host stress response. PK2 was found in complex with PKR and blocked kinase autophosphorylation in vivo, suggesting a mechanism of kinase inhibition mediated by interaction between truncated and intact kinase domains.

Original languageEnglish (US)
Pages (from-to)4164-4169
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number8
DOIs
StatePublished - Apr 14 1998

All Science Journal Classification (ASJC) codes

  • General

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