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Nucleic Acids Research, 2000, Vol. 28, No. 6 1407-1417
© 2000 Oxford University Press

A new double-stranded RNA-binding protein that interacts with PKR

Candace J. Coolidge and James G. Patton*

Department of Molecular Biology, Box 1820, Station B, Vanderbilt University, Nashville, TN 37235, USA

We have identified a 74 kDa double-stranded (ds)RNA-binding protein that shares extensive homology with the mouse spermatid perinuclear RNA-binding (Spnr) protein. p74 contains two dsRNA-binding motifs (dsRBMs) that are essential for preferential binding to dsRNA. Previously, dsRNA-binding proteins were shown to undergo homo- and heterodimerization, raising the possibility that regulation of activity could be controlled by interactions between different family members. Homodimerization is required to activate the dsRNA-dependent protein kinase PKR, whereas hetero­dimerization between PKR and other dsRNA-binding proteins can inhibit kinase activity. We have found that p74 also interacts with PKR, both the wild-type enzyme and a catalytically defective mutant (K296R). While co-expression of p74 and wild-type PKR in the yeast Saccharomyces cerevisiae did not alter PKR activity, co-expression of p74 and the catalytically defective K296R mutant surprisingly resulted in abnormal morphology and cell death in transformants that maintained a high level of p74 expression. These transformants could be rescued by overexpression of the {alpha}-subunit of wild-type eukaryotic translation initiation factor 2 (eIF2{alpha}), one of the known substrates for PKR. We hypothesize that competing heterodimers between p74–K296R PKR and eIF2{alpha}–K296R PKR may control cell growth such that stabilization of the p74–K296R PKR heterodimer induces abnormal morphology and cell death.

* To whom correspondence should be addressed. Tel: +1 615 322 4738; Fax: +1 615 343 6707; Email: james.g.patton@vanderbilt.edu


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