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CIPK9: a calcium sensor-interacting protein kinase required for low-potassium tolerance in Arabidopsis 被引量:23
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作者 Girdhar K Pandey Yong Hwa Cheongx +3 位作者 Beom-Gi Kim John J Grant Legong Li Sheng Luan 《Cell Research》 SCIE CAS CSCD 2007年第5期411-421,共11页
Potassium is one of the major macro-nutrients essential for a number of cellular processes in plants. Low potassium level in the soil represents a limiting factor for crop production. Recent studies have identified po... Potassium is one of the major macro-nutrients essential for a number of cellular processes in plants. Low potassium level in the soil represents a limiting factor for crop production. Recent studies have identified potassium transporters that are involved in potassium acquisition, and some of them are critical for potassium nutrition under low potassium conditions. However, little is understood on the molecular components involved in low potassium signaling and responses. We report here the identification ofa calcineurin B-like protein-interacting protein kinase (CIPK9) as a critical regulator of low potassium response in ,Arabidopsis. The CIPK9 gene was responsive to abiotic stress conditions, and its transcript was inducible in both roots and shoots by potassium deprivation. Disruption of CIPK9 function rendered the mutant plants hypersensitive to low potassium media. Further analysis indicated that K^+ uptake and content were not affected in the mutant plants, implying CIPK9 in the regulation of potassium utilization or sensing processes. 展开更多
关键词 CALCIUM calcineurin-b like protein protein kinase potassium nutrition signal transduction
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Quality-control method for the determination of biological activity of engineered calcineurin subunit B
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作者 Xinchang Shi Huan Yang +5 位作者 Li Xu Xiang Li Zongwen Huang Yudong Han Qun Wei Chunming Rao 《Science China(Life Sciences)》 SCIE CAS CSCD 2016年第6期584-588,共5页
The aim of this study was to establish a quality-control method for calcineurin subunit B(CNB) biological activity determinations. CNB enhances the p-nitrophenylphosphate(p NPP) dephosphorylating activity of calcineur... The aim of this study was to establish a quality-control method for calcineurin subunit B(CNB) biological activity determinations. CNB enhances the p-nitrophenylphosphate(p NPP) dephosphorylating activity of calcineurin subunit A Δ316 mutant(CNAΔ316). A series of CNB concentrations were fitted to a four-parameter equation to calculate the corresponding p NPP maximum dephosphorylation rates. Values were calculated based on biological activity references using a parallel line method. The method was then validated for accuracy, precision, linearity, linear range, sensitivity, specificity, and robustness. The recovery results were greater than 98%. Intra-plate precision was 6.7%, with inter-plate precision of 10.8%. The coefficient of determination was greater than 0.98. The linear range was 0.05–50 μg m L?1, with sensitivity of 50 μg m L?1. Tested cytokines did not induce CNAΔ316 dephosphorylation of p NPP. The chosen CNAΔ316 concentration range did not affect activity determinations. 展开更多
关键词 calcineurin subunit B biological activity method establishment method validation quality control
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