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

• Published in: Journal of integrative plant biology 2019-12, Vol.61 (12), p.1194-1200
• Main Authors: Zhang, Dajian, Guo, Xiaoyu, Xu, Yunyuan, Li, Hao, Ma, Liang, Yao, Xuefeng, Weng, Yuxiang, Guo, Yan, Liu, Chun‐Ming, Chong, Kang
• Format: Article
• Language: English
• Subjects: Adaptation, Physiological; Amino Acid Sequence; Base Sequence; Breeding; Calcineurin; Chilling; Cold Temperature; Cooling; Environmental stress; Kinases; Molecular structure; Mutation; Oryza - enzymology; Oryza - physiology; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Proteins - metabolism; Point mutation; Point Mutation - genetics; Protein Conformation; Protein kinase; Protein Kinases - metabolism; Proteins; Spectroscopy, Fourier Transform Infrared
• ISSN: 1672-9072; 1744-7909
• DOI: 10.1111/jipb.12800

Summary 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. 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. This point mutation of OsCIPK7 led to the conformational change, subsequently with an increase of protein kinase activity, thus conferred an increased tolerance to chilling stress.