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CSHL-led team identifies key decision-point at which cells with broken DNA repair themselves or die
Date:4/10/2009

t kinds of expertise coming together" in what he describes as "a lovely moment" of synthesis and discovery. An important collaborator in the work, C. David Allis, Ph.D., of the Rockefeller University, had recently published a paper in Nature describing a critical component of the DNA damage-repair signaling cascade. The Tonks-Allis collaboration, along with contributions from Seung Jun Kim, Ph.D., a protein crystallographer from the Korea Research Institute of Bioscience and Biotechnology, led to the assembly of a puzzle from pieces whose precise relation was not previously understood.

The parts of the puzzle include a protein called H2A.X, one of a species of proteins called histones that form structures around which DNA is "spooled" for dense packing in the cell nucleus. "David Allis showed us that this particular histone, which is found at those critical decision points called gamma-H2A.X foci, has phosphate groups added to its structure at particular points at the end of the protein. David demonstrated that another kind of protein --a kinase called WSTF -- attaches phosphate to critical site, a tyrosine residue, at the extreme end of the protein," Tonks explains..

"I was interested in the fact that when there is damage to double-stranded DNA catastrophic damage, such as when the strand breaks in two the phosphate molecule placed at the decision point by WSTF has to be removed in order for the cell to send out signals for DNA-repair enzymes to come to the scene."

The removal of phosphate groups from proteins is accomplished by a family of enzymes called phosphatases the focus of much research in Tonks' CSHL laboratory. Tonks is well known for having characterized the first of what has come to be understood as a large superfamily of protein tyrosine phosphatases, or PTPs enzymes that specifically remove phosphate molecules from amino acid residues called tyrosines. This function is critical in regulating cellular signaling in
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Contact: Peter Tarr
tarr@cshl.edu
516-367-8455
Cold Spring Harbor Laboratory
Source:Eurekalert

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