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 journalArticlepeer-review

    60 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

    Fingerprint

    Dive into the research topics of 'Disruption of cellular translational control by a viral truncated eukaryotic translation initiation factor 2α kinase homolog'. Together they form a unique fingerprint.

    Cite this