Multi-omic characterization of bifunctional peroxidase 4-coumarate 3-hydroxylase knockdown in Brachypodium distachyon provides insights into lignin modification associated pleiotropic effects (open access)

Multi-omic characterization of bifunctional peroxidase 4-coumarate 3-hydroxylase knockdown in Brachypodium distachyon provides insights into lignin modification associated pleiotropic effects

Article discusses how a bifunctional peroxidase enzyme, 4-coumarate 3-hydroxylase (C3H/APX), provides a parallel route to the shikimate shunt pathway for the conversion of 4-coumarate to caffeate in the early steps of lignin biosynthesis. Here, a multi-omic approach was used to characterize molecular changes resulting from C3H/APX-KD associated lignin modification and negative growth phenotype in Brachypodium distachyon.
Date: September 28, 2022
Creator: Shrestha, Him K.; Fichman, Yosef; Engle, Nancy L.; Tschaplinski, Timothy J.; Mittler, Ron; Dixon, R. A. et al.
System: The UNT Digital Library