J Integr Plant Biol. ›› 2019, Vol. 61 ›› Issue (12): 1194-1200.DOI: 10.1111/jipb.12800

• Breakthrough Reports •     Next Articles

OsCIPK7 point-mutation leads to conformation and kinase-activity change for sensing cold response

Dajian Zhang1,2†, Xiaoyu Guo1,2†, Yunyuan Xu1, Hao Li3, Liang Ma4, Xuefeng Yao1, Yuxiang Weng3, Yan Guo4, Chun-Ming Liu1 and Kang Chong1,2*   

  1. 1Key Laboratory of Plant Molecular Physiology, Institute of Botany, the Chinese Academy of Sciences, Beijing 100093, China
    2University of Chinese Academy of Sciences, Beijing 100049, China
    3Laboratory of Soft Matter Physics, Institute of Physics, the Chinese Academy of Sciences, Beijing 100190, China
    4State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China

    These authors contributed equally to this work.
    Email: Kang Chong (chongk@ibcas.ac.cn)
  • Received:2019-01-16 Accepted:2019-03-07 Online:2019-03-25 Published:2019-12-01

Abstract: 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.

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