Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance

Vijay Hegde, Mu Wang, Walter A. Deutsch

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

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 β-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 (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 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.

Original languageEnglish
Pages (from-to)121-126
Number of pages6
JournalDNA Repair
Volume3
Issue number2
DOIs
StatePublished - Feb 3 2004

Fingerprint

Surface Plasmon Resonance
Surface plasmon resonance
Protein Binding
DNA
DNA Repair
Repair
Lyases
Ribosomal Proteins
Protein Biosynthesis
Oligonucleotides
7,8-dihydro-8-oxoguanine
human RPS3 protein
Enzymes
Proteins

Keywords

  • Base excision DNA repair
  • DNA glycosylase
  • Protein-DNA interaction
  • SPR analysis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance. / Hegde, Vijay; Wang, Mu; Deutsch, Walter A.

In: DNA Repair, Vol. 3, No. 2, 03.02.2004, p. 121-126.

Research output: Contribution to journalArticle

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