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Published on January 30, 2008; 10.1104/pp.107.110189

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Received October 4, 2007
Accepted January 19, 2008

The native cyclobutane pyrimidine dimer photolyase of rice is phosphorylated

Mika Teranishi *, Kentaro Nakamura , Hiroshi Morioka , Kazuo Yamamoto , and Jun Hidema

Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, Sendai 980-8577, Japan; Department of Analytical and Biophysical Chemistry, Faculty of Medical and Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973, Japan; Department of Biomolecular Sciences, Graduate School of Life Sciences, Tohoku University, Sendai 980-8577, Japan

* Corresponding author; email: tera{at}ige.tohoku.ac.jp.

The cyclobutane pyrimidine dimer (CPD) is a major type of DNA damage induced by ultraviolet B (UVB) radiation. CPD photolyase, which absorbs blue/UVA light as an energy source to monomerize dimers, is a crucial factor for determining the sensitivity of rice to UVB light. Here, we purified native class II CPD photolyase from rice leaves. As the final purification step, CPD photolyase was bound to CPD-containing DNA conjugated to magnetic beads and then released by blue light irradiation. The final purified fraction contained 54- and 56-kDa proteins, whereas rice CPD photolyase expressed from E. coli was a single 55-kDa protein. Western blot analysis using anti-rice CPD photolyase antiserum suggested that both the 54- and 56-kDa proteins were the CPD photolyase. Treatment with protein phosphatase revealed that the 56-kDa native rice CPD photolyase was phosphorylated, whereas the E. coli-expressed rice CPD photolyase was not. The purified native rice CPD photolyase also had significantly higher CPD photorepair activity than the E. coli-expressed CPD photolyase. According to the absorption, emission, and excitation spectra, the purified native rice CPD photolyase possesses both a pterin-like chromophore and an FAD chromophore. The binding activity of the native rice CPD photolyase to thymine dimers was higher than that of the E. coli-expressed CPD photolyase. These results suggest that the structure of the native rice CPD photolyase differs significantly from that of the E. coli-expressed rice CPD photolyase, and the structural modification of the native CPD photolyase leads to higher activity in rice.






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