Regulation of the interferon-inducible protein kinase PKR and (2'-5')oligo(adenylate) synthetase by a catalytically inactive PKR mutant through competition for double-stranded RNA binding.

Abstract excerpt

The interferon-inducible double-stranded RNA-dependent protein kinase PKR has been suggested to function as a tumour suppressor gene product. Catalytically inactive mutants of PKR give rise to a tumorigenic phenotype when overexpressed in NIH-3T3 fibroblasts and this has been attributed to a dominant negative effect on the activity of the wild-type enzyme. Here we show that the mutant with Lys296 replaced by Arg,...

Topics

• 2',5'-Oligoadenylate Synthetase
• Binding, Competitive
• Interferons
• Mutation
• Protein Serine-Threonine Kinases
• RNA, Double-Stranded
• eIF-2 Kinase