| First Author | Kim SH | Year | 2005 |
| Journal | Biochem Biophys Res Commun | Volume | 328 |
| Issue | 4 | Pages | 962-7 |
| PubMed ID | 15707971 | Mgi Jnum | J:96083 |
| Mgi Id | MGI:3529384 | Doi | 10.1016/j.bbrc.2005.01.045 |
| Citation | Kim SH, et al. (2005) Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3. Biochem Biophys Res Commun 328(4):962-7 |
| abstractText | 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 MgCl(2) on AP DNA but not on UV-irradiated DNA. |
