Calcineurin B‐like interacting protein kinases (CIPKs) play important roles via environmental stress. However, less is known how to sense the stress in molecular structure conformation level. Here, an OsCIPK7 mutant via TILLING procedure with a point mutation in the kinase domain showed increased chilling tolerance, which could be potentially used in the molecular breeding. We found that this point mutation of OsCIPK7 led to a conformational change in the activation loop of the kinase domain, subsequently with an increase of protein kinase activity, thus conferred an increased tolerance to chilling stress.

中文翻译：

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OsCIPK7点突变可导致构象和激酶活性变化，从而感应到冷反应。

钙调神经磷酸酶B样相互作用蛋白激酶（CIPK）通过环境胁迫发挥重要作用。然而，如何在分子结构构象水平上感测应力的知之甚少。在这里，通过TILLING程序的OsCIPK7突变体在激酶结构域中具有点突变，显示出增强的耐寒性，这可能在分子育种中潜在地使用。我们发现，OsCIPK7的这一点突变导致激酶结构域的激活环发生构象变化，随后蛋白激酶活性增加，从而增强了对寒冷胁迫的耐受性。