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(Received for publication, June 13, 1995) PKR is an interferon (IFN)-induced serine/threonine protein
kinase that regulates protein synthesis through phosphorylation of
eukaryotic translation initiation factor-2 (eIF-2). In addition to its
demonstrated role in translational control, recent findings suggest
that PKR plays an important role in regulation of gene transcription,
as PKR phosphorylates I
Volume 270,
Number 43,
Issue of October 27, 1995 pp. 25426-25434
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Gene
B
upon double-stranded RNA treatment
resulting in activation of NF-
B DNA binding in vitro (Kumar, A., Haque, J., Lacoste, J., Hiscott, J., and Williams, B.
R. G.(1994) Proc. Natl. Acad. Sci. U. S. A. 91,
6288-6292). To further investigate the role of PKR in
transcriptional signaling, we expressed the wild type human PKR and a
catalytically inactive dominant negative PKR mutant in the murine pre-B
lymphoma 70Z/3 cells. Here, we report that expression of wild type PKR
had no effect on
-chain transcriptional activation induced by
lipopolysaccharide or IFN-. However, expression of the dominant
negative PKR mutant inhibited
gene transcription independently of
NF-
B activation. Phosphorylation of eIF-2
was not increased
by lipopolysaccharide or IFN-, suggesting that PKR mediates
gene transcriptional activation without affecting protein synthesis.
Our findings further support a transcriptional role for PKR and
demonstrate that there are at least two distinct PKR-mediated signal
transduction pathways to the transcriptional machinery depending on
cell type and stimuli, NF-
B-dependent and NF-
B-independent.
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