Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3

Sang Hwa Kim, Jae Yung Lee, Joon Kim

Research output: Contribution to journalArticlepeer-review

52 Citations (Scopus)


Mammalian rpS3, a ribosomal protein S3 with a DNA repair endonuclease activity, nicks heavily UV-irradiated DNA and DNA containing AP sites. RpS3 calls for a novel endonucleolytic activity on AP sites generated from pyrimidine dimers by T4 pyrimidine dimer glycosylase activity. This study revealed that rpS3 cleaves the lesions including AP sites, thymine glycols, and other UV damaged lesions such as pyrimidine dimers. This enzyme does not have a glycosylase activity as predicted from its amino acid sequence. However, it has an endonuclease activity on DNA containing thymine glycol, which is exactly overlapped with UV-irradiated or AP DNAs, indicating that rpS3 cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity acting as a base-damage-endonuclease. RpS3 cleaves supercoiled UV damaged DNA more efficiently than the relaxed counterpart, and the endonuclease activity of rpS3 was inhibited by MgCl2 on AP DNA but not on UV-irradiated DNA.

Original languageEnglish
Pages (from-to)962-967
Number of pages6
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2005 Mar 25

Bibliographical note

Funding Information:
We are deeply indebted to Dr. Stuart Linn at U.C. Berkeley for helpful discussion and this work was supported in part by KRF Grant C00073.


  • AP
  • DNA repair
  • UV endonuclease
  • rpS3

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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