title: Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress.
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.
authors.affiliation: Pennington Biomedical Research Center, Louisiana State University System, Baton Rouge, LA 70808, USA.
authors.forename: Sridevi
authors.initials: S
authors.lastname: Yadavilli
authors.forename: Vijay
authors.initials: V
authors.lastname: Hegde
authors.forename: Walter A
authors.initials: WA
authors.lastname: Deutsch
mesh_terms: D001483:Base Sequence; D002460:Cell Line; D004249:DNA Damage; D017931:DNA Primers; D048049:Extracellular Signal-Regulated MAP Kinases / Q000378:metabolism*; D006801:Humans; D016297:Mutagenesis, Site-Directed; D009153:Mutagens / Q000633:toxicity*; D010766:Phosphorylation; D021381:Protein Transport; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D017931:DNA Primers; D009153:Mutagens; D012269:Ribosomal Proteins; C044152:ribosomal protein S3; D048049:Extracellular Signal-Regulated MAP Kinases