Low-Temperature-Induced Expression of Rice Ureidoglycolate Amidohydrolase is Mediated by a C-Repeat/Dehydration-Responsive Element that Specifically Interacts with Rice C-Repeat-Binding Factor 3

文献类型: 外文期刊

第一作者: Li, Juan

作者: Li, Juan;Qin, Rui-Ying;Li, Hao;Xu, Rong-Fang;Yang, Ya-Chun;Ni, Da-Hu;Ma, Hui;Li, Li;Wei, Peng-Cheng;Yang, Jian-Bo

作者机构:

关键词: CRT/DRE element;low temperature stress;OsCBF3;transcriptional regulation;ureidoglycolate amidohydrolase

期刊名称:FRONTIERS IN PLANT SCIENCE ( 影响因子:5.753; 五年影响因子:6.612 )

ISSN: 1664-462X

年卷期: 2015 年 6 卷

页码:

收录情况: SCI

摘要: Nitrogen recycling and redistribution are important for the environmental stress response of plants. In non-nitrogen-fixing plants, ureide metabolism is crucial to nitrogen recycling from organic sources. Various studies have suggested that the rate-limiting components of ureide metabolism respond to environmental stresses. However, the underlying regulation mechanism is not well understood. In this report, rice uradoglycolate amidohydrolase (OsUAH), which is a recently identified enzyme catalyzing the final step of ureide degradation, was identified as low-temperature- (LT) but not abscisic acid- (ABA) regulated. To elucidate the LT regulatory mechanism at the transcriptional level, we isolated and characterized the promoter region of OsUAH (PosuAH). Series deletions revealed that a minimal region between 522 and 420 relative to the transcriptional start site was sufficient for the cold induction of PosuAH. Detailed analyses of this 103 bp fragment indicated that a C-repeat/dehydration-responsive (CRT/DRE) element localized at position 434 was essential for LT-responsive expression. A rice C-repeat-binding factors/DRE-binding proteins 1 (CBE5/DREB1s) subfamily member, OsCBF3, was screened to specifically bind to the CRT/DRE element in the minimal region both in yeast one hybrid assays and in in vitro gel shift analysis. Moreover, the promoter could be exclusively trans-activated by the interaction between the CRT/DRE element and OsCBF3 in vivo. These findings may help to elucidate the regulation mechanism of stress-responsive ureide metabolism genes and provide an example of the member specific manipulation of the CBF/DREB1 subfamily.

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