A shadow commander for flavonoid biosynthesis

February 28, 2020

Using a chalcone isomerase–like protein as a survival strategy

Plants moved from water to land about 450 million years ago and have acquired the ability to produce flavonoids to adapt to the terrestrial environment. In extent plants, flavonoids play important roles for stress adaptation and reproduction, and are also of great interest to humans as health beneficial compounds.

A joint research group including Tohoku University, Kanazawa University, the Institute for Basic Biology and RIKEN CSRS has discovered that chalcone isomerase–like protein (CHIL) binds to chalcone synthase (CHS), a key enzyme in flavonoid biosynthesis, and rectifies promiscuous chalcone synthase specificity towards flavonoid synthesis. Interestingly, CHIL is literally similar to a flavonoid biosynthetic enzyme, chalcone isomerase, but it is a non-enzymatic protein. The CHIL function to raise the flavonoid biosynthetic efficiency is conserved among land plants.

These findings have a profound impact on the understanding of metabolic strategies to adapt to the terrestrial environment and neofunctionalization of proteins during plant evolutionary process. It should also prove to be an essential factor for efficient production of flavonoids.

 

Original article
Nature Communications doi:10.1038/s41467-020-14558-9
T. Waki, R. Mameda, T. Nakano, S. Yamada, M. Terashita, K. Ito, N. Tenma, Y. Li, N. Fujino, K. Uno, S. Yamashita, Y. Aoki, K. Denessiouk, Y. Kawai, S. Sugawara, K. Saito, K. Yonekura-Sakakibara, Y. Morita, A. Hoshino, S. Takahashi, T. Nakayama,
"A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity".

Contact
Kazuki Saito; Group Drector
Keiko Sakakibara; Senior Scientist
Metabolomics Research Group