Micro-thermophoresis MST helps reveal the mechanism of action of important peptide hormones in plants
Micro Thermophoresis MST User Professor Tsinghua University, School of Life Sciences, Tsinghua University, Research Group, Institute of Genetics and Development, Chinese Academy of Sciences, Researcher, Yang Weicai Research Group, "Nature" published "Allosteric receptors of plant peptide hormone phytosulfokine receptor" (Allosteric receptor) A study paper (Nature 2015, 525, 265-268) reveals the molecular mechanism of recognition and receptor activation of the plant important peptide hormone phytosulfokine (PSK).
Plant peptide hormones, like plant classic hormones, have important regulatory effects on physiological activities such as growth and development of plants. PSK is a pentapeptide hormone containing two tyrosine sulfonation modifications that was discovered and studied earlier. It has extensive regulation in plant growth and development, stress resistance and innate immunity. PSK exerts its activity by binding to the receptor kinase PSKR on the cell membrane. However, the molecular mechanism by which PSK is recognized by the receptor PSKR and the subsequent receptor activation mechanisms need to be elucidated.
By studying the complex structure of PSKR extracellular domain and PSK complex, Chai Jijie's research group clarified the molecular mechanism of PSKR extracellular domain to identify PSK through its island region. In-depth structural analysis suggests that members of the SERK family may participate in the receptor activation of PSKR as co-receptors. This hypothesis was confirmed by in vitro biochemical experiments, and in collaboration with the research team of the Institute of Genetics and Development of the Chinese Academy of Sciences, Yang Weicai, the use of plant biochemistry and The genetic approach ultimately proved this hypothesis. This is also the discovery of new components on the PSK signal transduction pathway through structural biology. By analyzing and comparing and analyzing the structure of PSKR/PSK/SERK ternary complex and the PSKR structure alone, it is revealed that PSK can form a new interface with the co-receptor SERK by inducing the originally disordered receptor PSKR island region.
Nanotemper's micro-thermophoresis (MST) researchers measured PSKR and PSK affinity (Kd: 1.55 μM) significantly better than sulfonated-free dPSK (Kd: 41.5 μM), consistent with in vivo data (Figure a). In addition, the researchers used MST to identify multiple amino acids on PSKR that are critical for the recognition of PSK (Figure b).
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