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DNA Repair Activity of Human rpS3 is Operative to Genotoxic Damage in Bacteria  

JANG CHANG-YOUNG (Laboratory of Biochemistry, School of Life Sciences & Biotechnology, and Bioinstitute, Korea University)
LEE JAE YUNG (Department of Biology, Mokpo National University)
KIM JOON (Laboratory of Biochemistry, School of Life Sciences & Biotechnology, and Bioinstitute, Korea University)
Publication Information
Journal of Microbiology and Biotechnology / v.15, no.3, 2005 , pp. 484-490 More about this Journal
Abstract
Human ribosomal protein S3 (rpS3), which has a DNA repair endonuclease activity, is a multifunctional protein. This protein is involved in DNA repair, translation, and apoptosis. In particular, rpS3 has a lyase activity, which cleaves the phosphodiester bond of damaged sites such as cyclobutane pyrimidine dimers and AP sites. Here, using deletion analysis, we identified that the repair endonuclease domain resides in the C-terminal region (165-243 aa) of rpS3. We also found that ectopic expression of GST-rpS3 in bacterial strain BL21 promoted the resistance of these cells to ultraviolet (UV) radiation and hydrogen peroxide ($H_{2}O_{2}$) treatment. The repair domain of rpS3 was sufficient to exhibit the resistance to UV irradiation and recover cell growth and viability, showing that the repair activity of rpS3 is responsible for the resistance to UV irradiation. Our study suggests that rpS3 is able to process DNA damage in bacteria via its repair domain, showing the resistance to genotoxic stress. This implies that rpS3-like activity could be operative in bacteria.
Keywords
rpS3; DNA repair; repair domain; endonuclease; UV resistance;
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