UVB sensitivity and cyclobutane pyrimidine dimer ( CPD) photolyase genotypes in cultivated and wild rice species
UVB sensitivity and cyclobutane pyrimidine dimer ( CPD) photolyase genotypes in cultivated and wild rice species
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DOI：
10.1039/b719034d
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发表时间：
2008-03
影响因子：
3.1
通讯作者：
Y. Iwamatsu;C. Aoki;M. Takahashi;Mika Teranishi;Yuanying Ding;Chuanqing Sun;T. Kumagai;J. Hidema
中科院分区：
文献类型：
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作者：
Y. Iwamatsu;C. Aoki;M. Takahashi;Mika Teranishi;Yuanying Ding;Chuanqing Sun;T. Kumagai;J. Hidema
本文研究了两个栽培种（O. sativa和O. glaberrima）和3个野生种（O. barthii、黑尾野螟O. tagonalis和O. rufipogon）具有AA基因组的水稻，同时重点研究CPD光裂合酶活性和CPD光裂合酶基因型。虽然UVB敏感性，CPD光解酶活性，CPD光解酶基因型在这些水稻品种之间的差异很大，对UVB辐射的敏感性依赖于CPD光解酶的活性，无论草的形状，栖息地，或物种。根据CPD光裂合酶的活性，这里检测的水稻菌株明显地分为三组，菌株的活性很大程度上取决于126和296位的氨基酸残基，除了W1299菌株（O.属）。Sasanishiki菌株CPD光裂合酶的第126和296位氨基酸残基（O. sativa）中，酶活性最高的是谷氨酰胺（Gln），抗紫外线能力最强的是Gln。在位置126处从Gln到精氨酸（“Nori”型）的光裂合酶的氨基酸变化导致酶活性的降低。此外，位置296处的氨基酸从Gln变为组氨酸导致活性进一步降低。具有“Nori”型CPD光裂合酶的W1299菌株的活性在这里检测的菌株中最高，并且与Sasanishiki的活性相似。与Sasanishiki相比，W1299的CPD光解酶含有10个氨基酸取代。W1299 CPD光裂合酶中氨基酸残基的改变补偿了由位置126处的氨基酸取代引起的活性降低。了解不同CPD光裂合酶基因型的活性，将有助于培育改良的水稻品种。
We investigated the UVB-sensitivity in 12 rice strains belonging to two cultivated species ( O. sativa and O. glaberrima ) and three wild species ( O. barthii , O. meridionalis and O. rufipogon ) of rice possessing the AA genome, while focusing on the CPD photolyase activity and the genotypes of CPD photolyase. Although the UVB sensitivity, CPD photolyase activity, and CPD photolyase genotype varied widely among these rice species, the sensitivity to UVB radiation depended on the activity of the CPD photolyase, regardless of grass shape, habitat, or species. The rice strains examined here clearly divided into three groups based on the CPD photolyase activity, and the activity of the strains greatly depended on amino acid residues at positions 126 and 296, with the exception of the W1299 strain ( O. meridionalis ). The amino acid residues 126 and 296 of CPD photolyase in Sasanishiki strain ( O. sativa ), which showed higher enzymatic activity and more resistance to UVB, were glutamine (Gln) and Gln, respectively. An amino acid change at position 126 from Gln to arginine (“Nori”-type) in the photolyase led to a reduction of enzymatic activity. Additionally, an amino acid change at position 296 from Gln to histidine led to a further reduction in activity. The activity of the W1299 strain, which possesses a “Nori”-type CPD photolyase, was the highest among the strains examined here, and was similar to that of the Sasanishiki. The CPD photolyase of the W1299 contains ten amino acid substitutions, compared to Sasanishiki. The alterations in amino acid residues in the W1299 CPD photolyase compensated for the reduction in activity caused by the amino acid substitutions at positions 126. Knowledge of the activity of different CPD photolyase genotypes will be useful in developing improved rice cultivars.