Journal
DNA REPAIR
Volume 3, Issue 2, Pages 121-126Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dnarep.2003.10.004
Keywords
base excision DNA repair; DNA glycosylase; protein-DNA interaction; SPR analysis
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Funding
- NCI NIH HHS [P01 CA75426] Funding Source: Medline
- NIEHS NIH HHS [R01 ES07815] Funding Source: Medline
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The human ribosomal protein S3 (hS3) possesses multifunctional activities that are involved in both protein translation, as well as the ability of cleaving apurinic/apyrimidinic (AP) DNA via a beta-elimination reaction. We recently showed that hS3 also has a surprising binding affinity for an 7,8-dihydro-8-oxoguanine (8-oxoG) residue embedded in a 5' end labeled 37mer DNA oligonucleotide. To understand the interaction of hS3 and DNA templates containing 8-oxoG, we carried out real-time analysis using surface plasmon resonance (SPR). Notably, hS3 was found to have an apparent three orders of magnitude higher binding affinity (K-D) for 8-oxoG than the human N-glycosylase/AP lyase base excision repair (BER) enzyme OGG1. An even more dramatic five orders of magnitude higher binding affinity for AP DNA was found for hS3 as opposed to hOGG1. These results suggest that ribosomal protein hS3 may have a multifunctional role that may also affect functions associated with DNA base excision repair transactions. (C) 2003 Elsevier B.V. All rights reserved.
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