Low Temperature (10K) 25Mg Solid-State NMR of DNA Repair Proteins and Their
Complexes
EMSL Project ID
24991
Abstract
The chemistry central to the function of the DNA repair proteins apurinic/apyrimidic endonuclease 1 (APE1) and polymerase β (Pol β) is the chemistry of water activated by Mg2+. These proteins are key constituents of the base excision repair (BER) pathway, a process that plays a critical role in preventing the cytotoxic and mutagenic effects of most spontaneous, alkylation and oxidative DNA damage. The principal aim of the proposed research is to establish a relationship between 25Mg magnetic resonance parameters and the structure/function relationships for known Mg-dependent DNA repair proteins and extrapolating those relationships to DNA repair proteins where the role of the magnesium is less defined. This work is in collaboration with S. Wilson (Pol β - NIEHS) and D. Wilson III (APE1 -NIA). Due to the similarity of the questions and the proposed science, we have combined these efforts.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2007-05-23
End Date
2010-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Lipton AS, PD Ellis, and TE Polenova. 2009. "Quadrupolar Metal Nuclides in Bioinorganic Chemistry: Solid-State NMR Studies." In Encyclopedia of Magnetic Resonance. John Wiley & Sons, Ltd., Hoboken, NJ.
Lipton AS, RW Heck, SV Primak, DR McNeill, DM Wilson Iii, and PD Ellis. 2008. "Characterization of Mg2+ Binding to the DNA Repair Protein Apurinic/Apyrimidic Endonuclease 1 via Solid-State 25Mg NMR Spectroscopy." Journal of the American Chemical Society 130(29):9332-9341. doi:10.1021/ja0776881