The DNA repair domain of human rpS3 protects against photoaging by removing cyclobutane pyrimidine dimers

Hee Woong Yang, Hag Dong Kim, Joon Kim

Research output: Contribution to journalLetter

1 Citation (Scopus)

Abstract

Ribosomal protein S3 (rpS3) has endonuclease activity for DNA repair. In particular, rpS3 cleaves the phosphodiester bonds of damaged DNA. In this study, we show that the repair domain of rpS3 spans amino acids 144–189. We fused rpS3 with the transactivator of transcription (TAT) sequence to introduce the rpS3 repair domain into cells. We find that the TAT-rpS3 (aa: 144–189) peptide cleaves UV-induced cyclobutane pyrimidine dimers (CPDs) in cells. We also reveal that the TAT-rpS3 peptide reduces matrix metalloproteinase-1 (MMP-1) induction in UV-irradiated fibroblasts and increases cell migration activity. Taken together, our study suggests that penetration of the rpS3 repair domain into cells can cleave UV-induced CPDs and reduce MMP-1 expression induced by UV.

Original languageEnglish
JournalFEBS Letters
DOIs
Publication statusPublished - 2019 Jan 1

Keywords

  • Cell-penetrating peptides
  • cyclobutane pyrimidine dimers
  • DNA repair
  • matrix metalloproteinase-1
  • ribosomal protein S3
  • UV irradiation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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