HIGHLIGHTS
- who: Yang Gao from the Yang Gao, and Scott WNelson, From the Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa , Background: How nuclease activity of Mre, is controlled by Rad, is poorly understood. Results: Removal of the, terminal domain of , Mre, enhances its nuclease activity. Conclusions: The C terminus of Mre, is autoinhibitory, and complex formation with Rad, relieves this inhibition. Significance: This autoinhibition provides a mechanism for restricting the nuclease activity of Mre, in the absence of Rad50. Mre, and Rad, form a stable complex (MR) and work cooperatively in repairing DNA . . .
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