RRC ID 67118
Author Nakayasu M, Umemoto N, Akiyama R, Ohyama K, Lee HJ, Miyachi H, Watanabe B, Muranaka T, Saito K, Yukihiro S, Mizutani M.
Title Characterization of C-26 aminotransferase indispensable for steroidal glycoalkaloid biosynthesis.
Journal Plant J
Abstract Steroidal glycoalkaloids (SGAs) are toxic specialized metabolites found in members of the Solanaceae, such as potato (Solanum tuberosum) and tomato (S. lycopersicum). Major potato SGAs are α-solanine and α-chaconine, which are biosynthesized from cholesterol. Previously, we characterized two cytochrome P450 monooxygenases and a 2-oxoglutarate-dependent dioxygenase that function in hydroxylation at the C-22, C-26, and C-16α positions, while an aminotransferase responsible for the introduction of a nitrogen moiety into the steroidal skeleton remains uncharacterized. Here, we show that PGA4 encoding a putative γ-aminobutyrate aminotransferase is involved in SGA biosynthesis in potatoes. The PGA4 transcript was expressed at high levels in tuber sprouts, in which SGAs are abundant. Silencing the PGA4 gene decreased potato SGA levels and instead caused the accumulation of furostanol saponins. Analysis of the tomato PGA4 ortholog, GAME12, essentially provided the same results. Recombinant PGA4 protein exhibited catalysis of transamination at the C-26 position of 22-hydroxy-26-oxocholesterol using γ-aminobutyric acid as an amino donor. S. stipuloideum (PI 498120), which is a tuber-bearing wild potato species lacking SGA, was found to have a defective PGA4 gene expressing the truncated transcripts, and transformation of PI 498120 with functional PGA4 resulted in complementation of SGA production. These findings indicate that PGA4 is a key enzyme for transamination in SGA biosynthesis. The disruption of PGA4 function by genome editing will be a viable approach for accumulating valuable steroidal saponins in SGA-free potatoes.
Published 2021-7-17
DOI 10.1111/tpj.15426
PMID 34273198
IF 5.726
Tomato TOMJPF00001 (Micro-Tom)