Sugar starvation-regulated MYBS2 and 14-3-3 protein interactions enhance plant growth, stress tolerance, and grain weight in rice

DOI Web Site 2 Citations
  • Yi-Shih Chen
    Institute of Molecular Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan, Republic of China;
  • Tuan-Hua David Ho
    Institute of Plant and Microbial Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan, Republic of China;
  • Lihong Liu
    Institute of Molecular Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan, Republic of China;
  • Ding Hua Lee
    Institute of Plant and Microbial Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan, Republic of China;
  • Chun-Hua Lee
    Department of Life Sciences, National Central University, Jhongli City, 320 Taoyuan County, Taiwan, Republic of China;
  • Yi-Ru Chen
    Institute of Molecular Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan, Republic of China;
  • Shu-Yu Lin
    Institute of Biological Chemistry, Academia Sinica, Nankang, 115 Taipei, Taiwan, Republic of China
  • Chung-An Lu
    Department of Life Sciences, National Central University, Jhongli City, 320 Taoyuan County, Taiwan, Republic of China;
  • Su-May Yu
    Institute of Molecular Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan, Republic of China;

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<jats:title>Significance</jats:title> <jats:p> As autotrophic organisms, sugar status in plants must be constantly monitored and reacted to in order to maintain sugar homeostatic states crucial for growth regulation, environmental stress tolerance, and productivity. α-Amylase (αAmy) is the key enzyme hydrolyzing starch into sugars and is regulated by sugar levels; it is induced by sugar starvation but repressed by sugar provision. Two MYBs compete for binding to the same <jats:italic>αAmy</jats:italic> promoter element to regulate this process, with MYBS1 promoting and MYBS2 repressing <jats:italic>αAmy</jats:italic> expression. Induction of <jats:italic>αAmy</jats:italic> expression by suppressing MYBS2 enhances stress tolerance and productivity. Phosphorylation of MYBS2 is critical for regulating its sugar-dependent nucleocytoplasmic shuttling and interactions with 14-3-3 proteins, representing a regulatory mechanism for reversible gene expression by sugar status. </jats:p>

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