Assessment of the Role of PAL in Lignin Accumulation in Wheat (Tríticum aestívum L.) at the Early Stage of Ontogenesis

Int J Mol Sci. 2021 Sep 12;22(18):9848. doi: 10.3390/ijms22189848.

Abstract

The current study evaluates the role of phenylalanine ammonia-lyase (PAL) and the associated metabolic complex in the accumulation of lignin in common wheat plants (Tríticum aestívum L.) at the early stages of ontogenesis. The data analysis was performed using plant samples that had reached Phases 4 and 5 on the Feekes scale-these phases are characterized by a transition to the formation of axial (stem) structures in cereal plants. We have shown that the substrate stimulation of PAL with key substrates, such as L-phenylalanine and L-tyrosine, leads to a significant increase in lignin by an average of 20% in experimental plants compared to control plants. In addition, the presence of these compounds in the nutrient medium led to an increase in the number of gene transcripts associated with lignin synthesis (PAL6, C4H1, 4CL1, C3H1). Inhibition was the main tool of the study. Potential competitive inhibitors of PAL were used: the optical isomer of L-phenylalanine-D-phenylalanine-and the hydroxylamine equivalent of phenylalanine-O-Benzylhydroxylamine. As a result, plants incubated on a medium supplemented with O-Benzylhydroxylamine were characterized by reduced PAL activity (almost one third). The lignin content of the cell wall in plants treated with O-Benzylhydroxylamine was almost halved. In contrast, D-phenylalanine did not lead to significant changes in the lignin-associated metabolic complex, and its effect was similar to that of specific substrates.

Keywords: D-phenylalanine; L-phenylalanine; L-tyrosine; O-Benzylhydroxylamine; PAL; POD; Triticum aestivum L.; lignin.

MeSH terms

  • Ammonia-Lyases / metabolism
  • Biomass
  • Lignin / biosynthesis*
  • Phenylalanine Ammonia-Lyase / antagonists & inhibitors
  • Phenylalanine Ammonia-Lyase / metabolism*
  • Triticum / enzymology*
  • Triticum / growth & development

Substances

  • Lignin
  • Ammonia-Lyases
  • L-tyrosine ammonia-lyase
  • Phenylalanine Ammonia-Lyase