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. Knockdown of C3H/APX (c3h/apx) expression has been shown to reduce the lignin content in Brachypodium distachyon. However, like many other lignin-modified plants, c3h/apx plant shows unpredictable pleiotropic phenotypes, including stunted growth, delayed senescence, and reduced seed yield. A system-wide level understanding of altered biological processes in lignin-modified plants can help pinpoint the lignin-modification associated growth defects to benefit future studies aiming to negate the yield penalty. Here, a global proteomics measurement of the stem tissue of the model grass Brachypodium distachyon was used to investigate the underlying mechanism of c3h/apx-associated lignin modification and negative growth phenotype. Our findings demonstrate that C3H/APX knockdown in Brachypodium stems substantially alters the abundance of enzymes implicated in the phenylpropanoid biosynthetic pathway and disrupt cellular redox homeostasis. Moreover, it elicits plant defense response associated with intracellular kinases and phytohormone-based signaling to facilitate growth-defense trade-offs. A deeper understanding along with potential targets to mitigate the pleiotropic phenotypes identified in this study could aid to increase the economic feasibility of lignocellulosic biofuel production.
[doi:10.25345/C5GF0N05M]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: LC-MS/MS, comparative proteomics, Brachypodium distachyon, lignin biosynthesis, cytosolic ascorbate peroxidase
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Jaime Barros, University of North Texas, United States Paul E. Abraham, Oak Ridge National Laboratory, United States |
Submitting User: | CBI_lignin_c3h |
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