Quantitative proteomics analysis reveals proteins and pathways associated with anthocyanin accumulation in barley

Food Chem. 2019 Nov 15:298:124973. doi: 10.1016/j.foodchem.2019.124973. Epub 2019 Jun 12.

Abstract

The aim of the present study was to explore the underlying mechanisms involved in anthocyanin biosynthesis in purple, blue, and white barley using quantitative proteomics analysis. We identified the differences in protein expression and related functions involved in anthocyanin biosynthesis in purple, blue, and white barley (named H, M, and L groups, respectively, based on their anthocyanin content) using TMT-liquid chromatography/mass spectroscopy-based proteomic methods. Totally, 297, 300, 254, and 1421 differentially expressed proteins (DEPs) were found in H vs. L, H vs. M, L vs. M, and H vs. L vs. M groups, respectively. Six clusters of proteins from the 1421 DEPs were mainly involved in carbon metabolism, amino acid and secondary metabolite biosynthesis, and metabolic pathways. Several proteins were validated using parallel reaction monitoring. The proteins involved in amino acid biosynthesis, carbon metabolism, metabolic pathways, and phenylpropanoid biosynthesis were responsible for the color differences in the three barley varieties.

Keywords: Anthocyanin; Color; Highland barley; Quantitative proteomics.

MeSH terms

  • Anthocyanins / metabolism*
  • Chromatography, Liquid
  • Hordeum / metabolism*
  • Pigmentation
  • Plant Proteins / analysis*
  • Plant Proteins / metabolism*
  • Proteomics / methods
  • Tandem Mass Spectrometry

Substances

  • Anthocyanins
  • Plant Proteins