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OsCML16 interacts with a novel CC-NBS-LRR protein OsPi304 in the Ca/Mg dependent and independent manner in rice.

Biochem. Biophys. Res. Commun.. 2018-09; 
YangJun,JiLingxiao,ZhuBohua,YuanXinjie,JinDeming,XieGuos
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Peptide Synthesis … 2.6. The in vitro peptide-binding assay. To further verify the target sites of candidate proteins to interact with OsCML16, two CaM-binding domain (CaMBD) peptide sequences of OsPi304 protein were predicted, and synthesized by GenScript (Nanjing, China) … Get A Quote

摘要

In plants, many target proteins of calmodulins (CaMs) have been identified in cellular metabolism and responses. However, calmodulin-like proteins (CMLs) and their target proteins have not been discovered in stress responses in rice. In this study, a novel CC-NBS-LRR protein was obtained in screening a cold stress rice seedlings yeast cDNA library with OsCML16 as bait. Furthermore, yeast two-hybrid and BiFC assays demonstrated that the full length, CC region in the N-terminus and LRR in the C-terminus of Pi304 protein could interact with OsCML16. More interestingly, OsCML16 bound to the 1-10 motif rather than 1-14 motif in the Ca or Mg dependent manner in vitro. In addition, transcript levels of ... More

关键词

CC-NBS-LRR protein,Calmodulin-like protein,Cold stress,Interaction,
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