DNA repair process revealed
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March 4, 2002—Two scientists at the Pacific Northwest National Laboratory, H. Peter Lu and Eric J. Ackerman, have successfully applied single-molecule spectroscopy to study the interactions of proteins and DNA to better understand how DNA is repaired. They are developing advanced chemical physics tools to study one of the first steps of this process, namely how the damaged DNA is recognized so that it can then be repaired.
All known life forms spend a considerable portion of their energy on some aspect of making and repairing their cellular DNA. Damaged DNA that is not repaired properly can lead to mutations. In humans, it is estimated that each cell must repair anywhere from tens of thousands to one million damaged sites in its DNA every day.
Scientists have been doing single molecule microscopy for only about 5 years and this is the first research focused on the interactions between DNA and DNA repair process to better understand how the repair mechanism works and why it occasionally fails.
"Instead of seeing an average of how large numbers of molecules of DNA and repair proteins interact, we are now able to see how a complex consisting of single-molecules interacts. This gives us a much better understanding of the range of interactions that are possible," said Eric J. Ackerman.
More than one protein is involved in the repair process, and more than one protein is involved in the damage-recognition process. With an understanding of which proteins are involved, the next step is to learn the molecular details of what the proteins do and how they do it.
"Research may one day augment the repair process and possibly lead to new ways to prevent cancer and other abnormalities," Lu said.
Media contact: PNNL Media Relations, pnl.media.relations@pnl.gov, (509) 375-3776
Technical contacts: H. Peter Lu, PNNL Chemical Structure and Dynamics, Peter.Lu@pnl.gov; or Eric J. Ackerman, PNNL Cellular Observatory, eric.ackerman@pnl.gov
Related Web Links
"Identification of Intrinsic Order and Disorder in the
DNA Repair Protein XPA," Iakoucheva LM, Kimzey AL, Masselon
CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith
RD, Ackerman EJ, Protein Science, 10, 560-571
(March 2001). [Abstract]
[Subscription required for full text]
"Aberrant mobility phenomena of the DNA repair protein
XPA," Iakoucheva LM, Kimzey AL, Masselon CD, Smith RD,
Dunker AK, and Ackerman EJ, Protein Science
10(7):1353-1362 (July 2001). [Abstract]
[Subscription required for full text]
Funding: This study was supported by the Chemical Sciences Division of the U.S. Department of Energy's Office of Basic Energy Sciences. Development of the single-molecule spectroscopy was supported by the Office of Biological and Environmental Research.
Pacific Northwest National Laboratory is a DOE research facility and delivers breakthrough science and technology in the areas of environment, energy, health, fundamental sciences and national security. Battelle, based in Columbus, Ohio, has operated the laboratory for DOE since 1965.
The William R. Wiley Environmental Molecular Sciences Laboratory (EMSL) [], the Department of Energy's newest national scientific user facility, is located at Pacific Northwest National Laboratory (PNNL) in Richland, Washington. The EMSL is operated by PNNL for the DOE Office of Biological and Environmental Research.
Author: Mike Berriochoa is the Communications Manager for Pacific Northwest National Laboratory's Fundamental Science Division. He works closely with scientists to help them communicate their accomplishments to a broad audience. He has an extensive background in media relations and broadcast journalism. For more science news, see PNNL's News & Publications