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Modeling lignin biosynthesis from proteomics and isotopic labeling data in Brachypodium distachyon

ABSTRACT: Previous studies suggest the existence of parallel biosynthetic routes to the building blocks of lignin. Here, using the model grass Brachypodium distachyon, we investigated these routes through a combined proteomics and isotope labeling approach. The key enzymes involved in the formation of phenolic acids L-phenylalanine/tyrosine ammonia-lyase (PTAL), p-coumarate 3-hydroxylase (C3H) and caffeic acid 3-O-methyltransferase (COMT) were among the most abundant of the 11,417 proteins identified in mature stems. A set of double RNAi-knockdown lines targeting putative parallel monolignol pathways did not produce additive effects on lignin deposition or growth defects, but instead induced pronounced proteome changes associated with oxidative stress and vitamin E synthesis. 13C-Labeling data, metabolic flux analysis and in situ hybridization experiments supported distinct but partially overlapping routes from L-phenylalanine and L-tyrosine into different lignin subunits and flavonoid classes associated with distinct cellular localization. These results provide a deeper understanding of the lignification process in grasses.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Brachypodium Distachyon (ncbitaxon:15368)

SUBMITTER: Paul E. Abraham

PROVIDER: MSV000087614 | MassIVE | Fri Jun 11 08:57:00 BST 2021

SECONDARY ACCESSION(S): PXD026665

REPOSITORIES: MassIVE

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