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Mechanism of mutant histone protein in childhood brain cancer revealed
Date:4/1/2013

ery amino acid in histones matters,'" says Allis, who is the Joy and Jack Fishman Professor. "These studies underscore just how true that may be."

The researchers went on to demonstrate that the reduction in methylation of normal H3 histones results from interference with activity of a methyltransferase called PRC2 by the mutant histone. Methylation of normal H3 by PRC2 leads to repression of genes involved in cellular growth pathways. Without methylation, genes involved in these pathways likely become activated, promoting the growth of tumors in DIPG. Allis and Lewis received funding from the National Institutes of Health and the Starr Cancer Consortium. Key collaborators in this work included Oren Becher at Duke University Medical Center and Tom Muir at Princeton University and their colleagues.

"Our finding provides us with a useful tool for probing biological processes," says Lewis. "This also tells us how to inhibit enzymes, which could lead to the development of pharmaceuticals that mimic the action of these mutants."

"We now have a model for the promotion of brain stem cancers through aberrant epigenetic silencing through the inhibition of PRC2 by a mutant histone," says Allis. "We have uncovered a potentially useful mechanism to exclusively inhibit individual SET-domain methyltransferases, and conceivably other chromatin-modifying enzymes, implicated in a variety of malignancies."


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Contact: Joseph Bonner
joseph.bonner@rockefeller.edu
212-327-8998
Rockefeller University
Source:Eurekalert

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