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Mouse work: New insights on a fundamental DNA repair mechanism
Date:3/4/2010

3 (99 percent identical to the human variant), and then prepare a truncated version of it that was small enough to dissolve in solution for analysis but large enough to retain the portion of the protein that recognizes and excises DNA lesions.

Using a technique they developed for rapidly analyzing such enzymes, NIST researchers Dizdaroglu and Pawel Jaruga mixed the modified protein with sample DNA that had been irradiated to produce large numbers of random base lesions. Because glycosylases work by snipping off damaged bases, a highly sensitive analysis of the solution after the DNA has been removed can reveal just which lesions are attacked by the enzyme, and with what efficiency. The NIST results closely matched independent tests by others in the team that match the enzyme against short lengths of DNA-like strands with a single specific target lesion.

In addition to finally confirming the glycosylase nature of NEIL3, says UVM team leader Susan Wallace, tests of the enzyme in a living organisma tailored form of E. coli designed to have a very high mutation ratehad an unexpected bonus. Measurements at NIST showed that NEIL3 is extremely effective at snipping out a particular type of lesion called FapyGua** and seems to dramatically reduce mutations in the bacterium, a result that points both to the effectiveness of NEIL3 and the potentially important role of FapyGua in causing dangerous mutations in DNA.


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Contact: Michael Baum
michael.baum@nist.gov
301-975-2763
National Institute of Standards and Technology (NIST)
Source:Eurekalert

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