Enzyme Complexes of Ptr4CL and PtrHCT Modulate Co-enzyme A Ligation of Hydroxycinnamic Acids for Monolignol Biosynthesis in Populus trichocarpa
Journal
Frontiers in Plant Science
Journal Volume
12
Pages
727932
Date Issued
2021
Author(s)
Chien-Yuan Lin
Yi Sunn
Jina Song
Hsi-Chuan Che
Rui Shi
Chenmin Yang
Jie Liu
Sermsawat Tunlaya-Anukit
Baoguang Liu
Philip L. Loziuk
Cranos M. Williams
David C. Muddiman
Ronald R. Sederoff
Jack P. Wang
Vincent L. Chiang
Abstract
Co-enzyme A (CoA) ligation of hydroxycinnamic acids by 4-coumaric acid:CoA ligase (4CL) is a critical step in the biosynthesis of monolignols. Perturbation of 4CL activity significantly impacts the lignin content of diverse plant species. In Populus trichocarpa, two well-studied xylem-specific Ptr4CLs (Ptr4CL3 and Ptr4CL5) catalyze the CoA ligation of 4-coumaric acid to 4-coumaroyl-CoA and caffeic acid to caffeoyl-CoA. Subsequently, two 4-hydroxycinnamoyl-CoA:shikimic acid hydroxycinnamoyl transferases (PtrHCT1 and PtrHCT6) mediate the conversion of 4-coumaroyl-CoA to caffeoyl-CoA. Here, we show that the CoA ligation of 4-coumaric and caffeic acids is modulated by Ptr4CL/PtrHCT protein complexes.
Subjects
BiFC; metabolic flux; monolignol biosynthesis; Populus trichocarpa; protein interaction; wood formation
SDGs
Publisher
Frontiers Media S.A.
Type
journal article