Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

Sridevi Yadavilli, Vijay Hegde, Walter A. Deutsch

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

Besides its role in translation and ribosome maturation, human ribosomal protein S3 (hS3) is implicated in DNA damage recognition as reflected by its affinity for abasic sites and 7,8-dihydro-8-oxoguanine (8-oxoG) residues in DNA in vitro. Here, we demonstrate that hS3 is capable of carrying out both roles by its ex vivo translocation from the cytoplasm to the nucleus as a consequence of genotoxic stress. The translocation of hS3 is dependent on ERK1/2-mediated phosphorylation of a threonine residue (T42) of hS3. Two different ectopically expressed site-directed mutants of T42 failed to respond to conditions of genotoxic stress, thus providing a link between DNA damage and ERK1/2 dependent phosphorylation of hS3. Lastly, hS3 was traced in exposed cells to its co-localization with 8-oxoG foci, raising the possibility that hS3 is a member of a cellular DNA damage response pathway that results in its interaction with sites of DNA damage.

Original languageEnglish
Pages (from-to)1453-1462
Number of pages10
JournalDNA Repair
Volume6
Issue number10
DOIs
StatePublished - Oct 1 2007

Keywords

  • Base excision repair
  • ERK
  • Genotoxic stress
  • Nuclear translocation
  • Ribosomal protein S3

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