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DNA repair process revealed
PNNL has developed highly sensitive single-molecule spectroscopy to allow scientists to study the binding of DNA repair proteins (red/green molecule) to DNA in real time. The bright spot on the DNA helix is a synthetically inserted fluorescent dye molecule that simulates a defect of the DNA.
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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.
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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
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