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Originally published In Press as doi:10.1074/jbc.M004481200 on October 18, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1634-1642, January 12, 2001
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Sequence-specific DNA Binding Activity of RNA Helicase A to the p16INK4a Promoter*

Sanna Myöhänen and Stephen B. BaylinDagger

From the Johns Hopkins Oncology Center, Baltimore, Maryland 21231

p16INK4a is frequently altered in human cancer, often through epigenetically mediated transcriptional silencing. However, little is known about the transcriptional regulation of this gene. To learn more about such control, we initiated studies of proteins that bind to the promoter in cancer cells that do, and do not, express the gene. We identify RNA helicase A (RHA) as a protein that binds much better to the p16INK4a promoter in the expressing cells. RHA has not previously been characterized to manifest sequence-specific DNA interaction but does so to the sequence 5' CGG ACC GCG TGC GC 3' in the p16INK4a promoter. The Drosophila homologue to RHA, maleless (Mle), functions in the fly for 2-fold activation of male X-chromosome genes. In our experimental setting, RHA induces a similar modest up-regulation of the p16INK4a promoter that is dependent upon its sequence-specific interaction. Mle colocalizes with hyperacetylated H4Ac16 on the X-chromosome and some autosomal loci. The decreased binding of RHA to p16INK4a in our cells, where the gene is transcriptionally inactive, is associated with decreased amounts of RHA that immunoprecipitate with acetylated lysine antibodies. Finally, we show RHA to be a cellular substrate for caspase-3, which decreases its sequence-specific binding to p16INK4a by cleavage of the N terminus. Thus, we have identified a new protein interaction with the p16INK4a promoter that involves an important protein for transcriptional modulation. This interaction is decreased in cancer cells, where this gene is aberrantly transcriptionally silent.

* This work was supported in part by a Public Health Service Grant (R01 CA43318) from the NCI, National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 410-955-8506; Fax: 410-614-9884; E-mail: sbaylin@jhmi.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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