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A more recent version of this article appeared on February 10, 2006
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Papers In Press, published online ahead of print December 8, 2005
J. Biol. Chem, 10.1074/jbc.M510612200
Submitted on September 28, 2005
Revised on November 21, 2005
Accepted on December 8, 2005

Activation of the RNA-dependent protein kinase PKR promoter in the absence of interferon is dependent upon Sp proteins

Sonali Das, Simone V. Ward, Robert S. Tacke, Guntrum Suske, and Charles E. Samuel

Molecular, Cellular and Developmental Biology, University of California, Santa Barbra, Santa Barbara, California 93106-9610

Corresponding Author: samuel{at}lifesci.ucsb.edu

The protein kinase regulated by RNA (PKR) is interferon (IFN) inducible and plays important roles in many cellular processes including virus multiplication, cell growth and apoptosis. The TATA-less PKR promoter possesses a novel 15-bp DNA element (KCS) unique to the human and mouse PKR genes that is conserved in sequence and position. We found that two Sp-family of transcription factors, Sp1 and Sp3, bind at the KCS element. Their involvement was analyzed in the activation of basal and IFN inducible PKR promoter activity. Both the small and large isoforms of Sp3 co-purified with KCS protein binding activity (KBP) using nuclear extracts from HeLa cells not treated with IFN. Two forms of KBP complex were demonstrated by EMSA analysis; one contained Sp1 and the other Sp3. In mouse cells null for all Sp3 isoforms, PKR expression was reduced to ~50% that of wild-type cells in the absence of IFN. The IFN inducible expression of PKR, however, was Sp3-independent, but STAT1- and JAK1-dependent. Over-expression of Sp1 in human U cells resulted in increased PKR promoter activity. In Drosophila SL2 cells lacking Sp proteins, both Sp1 and Sp3 large but not small isoforms activated PKR promoter expression, with the Sp1-mediated activation dominant. Mutational analysis of the PKR promoter region indicated a cooperative interaction between two different Sp sites, one of which is within the KCS element. These results establish that, in the absence of IFN treatment, activation of PKR basal expression is mediated by Sp1 and Sp3 proteins in a cooperative manner.


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