Key result
Viroid infection in plants induces differential phosphorylation of an Mr 68,000 host-encoded protein that is immunologically related to a human dsRNA-dependent protein kinase.
Identifies a plant host protein phosphorylated during viroid infection that is similar to mammalian dsRNA-dependent protein kinases involved in regulating protein synthesis and viral replication.
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Suggests conserved antiviral kinase pathways across kingdoms; leaves open any role in plant defense or human viral regulation.
Viroids are very small, unencapsidated RNAs that replicate and induce severe disease in plants without encoding for any proteins. The mechanisms by which the viroid RNA regulates these events and interacts with host factors are unknown. An Mr 68,000 host-encoded protein has been identified that is differentially phosphorylated in extracts from viroid-infected and mock-inoculated tissues. This phosphoprotein is immunologically related to a double-stranded (ds) RNA-dependent protein kinase from virus-infected, interferon-treated human cells. Further, nucleotide photoaffinity labeling indicates that the protein has an ATP binding site. This protein is similar to dsRNA-dependent protein kinases implicated in mammalian systems in the regulation of protein synthesis and virus replication.
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Hiddinga et al. (1988) studied Viroid infection. Viroid infection vs. Mock-inoculated tissues was evaluated on Differential phosphorylation of an Mr 68,000 host-encoded protein. Viroid infection in plants induces differential phosphorylation of an Mr 68,000 host-encoded protein that is immunologically related to a human dsRNA-dependent protein kinase.
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