Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1

Vijay Hegde, Mu Wang, Walter A. Deutsch

Research output: Contribution to journalArticle

51 Scopus citations

Abstract

The human ribosomal protein S3 (hS3) possesses associated activities that suggest alternative roles beyond its participation in protein translation. For example, it is capable of cleaving apurinic/ apyrimidinic (AP) DNA via a β-elimination reaction, an activity that is missing in partially purified extracts of xeroderma pigmentosum group-D fibroblasts. In a recent study, we showed by surface plasmon resonance (SPR) that hS3 also has a very high apparent binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG) and AP sites in DNA. Using the same SPR technology, it is shown here that hS3 positively interacts with the human base excision repair (BER) enzymes N-glycosylase/AP lyase OGG1 and APE/Ref-1. Using a DNA substrate that allows for the detection of 8-oxoG repair, we also show that hOGG1 N-glycosylase activity becomes increasingly more robust in the presence of hS3. Human S3 was found to co-immunoprecipitate with both hOGG1 and APE/Ref-1, indicating that these proteins physically interact with one another. These results raise the possibility that hS3 not only functions as a ribosomal protein but, in addition, may influence repair activities at sites of DNA damage.

Original languageEnglish
Pages (from-to)14211-14217
Number of pages7
JournalBiochemistry
Volume43
Issue number44
DOIs
StatePublished - Nov 9 2004

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