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- W3043403276 abstract "1558 The human ribosomal protein S3 (hS3) possesses multifunctional activities that are involved in both protein translation, as well as the ability to cleave apurinic/apyrimidinic (AP) DNA via a β-elimination reaction. Unlike its Drosophila homologue, however, hS3 does not contain an N-glycosylase activity for the liberation of 8-oxoG residues in oxidatively-damaged DNA. On the other hand, hS3 was found to bind to an 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). Using this technique, hS3 was found to have an apparent three orders of magnitude higher binding affinity (KD) for 8-oxoG than the human N-glycosylase/AP lyase base excision repair (BER) enzyme OGG1. An even more dramatic five orders of magnitude apparent higher binding affinity for AP DNA was found for hS3 as opposed to hOGG1. Tests were also conducted to determine if hS3 interacted with proteins associated with BER. Results using SPR analysis showed that hS3 positively interacts with the DNA BER enzymes hOGG1 and human APE/Ref-1. A physical interaction between hS3 and the BER enzymes was further documented through co-immunoprecipitation experiments. The human S3 has also been previously implicated in nucleotide excision repair (NER), where its AP lyase expression is totally absent in xeroderma pigmentosum group-D fibroblasts. Taken together, these results suggest that hS3 may possibly be involved in cross-talk between BER and NER." @default.
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- W3043403276 date "2004-04-01" @default.
- W3043403276 modified "2023-09-26" @default.
- W3043403276 title "The human ribosomal protein S3 binds to 8-oxoguanine residues in DNA and interacts with the base excision repair proteins hAPE/Ref-1 and hOGG1" @default.
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