Abstract

BackgroundFlour quality is largely determined by the gluten proteins, a complex mixture of proteins consisting of high molecular weight-glutenin subunits (HMW-GS), low molecular weight-glutenin subunits (LMW-GS), and α-, γ-, and ω-gliadins. Detailed proteomic analyses of the effects of fertilizer and high temperature on individual gliadin and glutenin protein levels are needed to determine how these environmental factors influence flour quality.ResultsWheat plants (Triticum aestivum L. cv. Butte 86) were grown in greenhouses under moderate and high temperature regimens with and without post-anthesis fertilizer. Quantitative two-dimensional gel electrophoresis was used to construct accumulation profiles in developing endosperm for the entire complement of gluten proteins identified previously by tandem mass spectrometry. Amounts of individual gliadins and glutenins were also determined in flour produced under each of the regimens. Under all environmental regimens, most HMW-GS, LMW-GS, γ- and ω-gliadins accumulated rapidly during early stages of grain development and leveled off during middle stages of development. A subset of LMW-GS showed a second distinct profile, accumulating throughout development, while α-gliadins showed a variety of accumulation profiles. In flour, fourteen distinct gluten proteins responded similarly to fertilizer, high temperature, and high temperature plus fertilizer. The majority of HMW-GS and ω-gliadins and some α-gliadins increased while two LMW-GS and a minor γ-gliadin decreased. Fertilizer did not influence gluten protein accumulation under high temperature conditions. Additionally, the effects of fertilizer and high temperature were not additive; very few changes were observed when plants that received fertilizer were subjected to high temperature.ConclusionsAlthough post-anthesis temperature and fertilizer have very different effects on grain development and yield, the two treatments elicit surprisingly similar effects on the accumulation of gluten proteins. The similarity of the responses to the different treatments is likely due to source-sink activities of nitrogen reserves in the wheat plant. Because each protein that showed a response in this study is linked to a gene sequence, the work sets the stage for transgenic studies that will better elucidate the roles of specific proteins in flour quality and in the response to the environment.

Highlights

  • Flour quality is largely determined by the gluten proteins, a complex mixture of proteins consisting of high molecular weight-glutenin subunits (HMW-GS), low molecular weight-glutenin subunits (LMW-GS), and α, γ, and ω-gliadins

  • Because the Butte 86 proteome map links gluten proteins to gene sequences, the goal of this study was to identify genes encoding proteins that respond to fertilizer and high temperature that can be used in transgenic approaches to determine the roles of specific proteins in flour quality and in the response of the grain to environmental cues

  • To distinguish responses to temperature from those of fertilizer, plants were grown under 24/17°C and 37/28°C regimens without and with post-anthesis fertilizer. Two-dimensional gel electrophoresis (2-DE) spots identified as HMW-GS, ω-gliadins or γ-gliadins generally showed expression profiles characteristic of each protein group while spots identified as α-gliadins showed a variety of expression profiles

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Summary

Introduction

Flour quality is largely determined by the gluten proteins, a complex mixture of proteins consisting of high molecular weight-glutenin subunits (HMW-GS), low molecular weight-glutenin subunits (LMW-GS), and α-, γ-, and ω-gliadins. Detailed proteomic analyses of the effects of fertilizer and high temperature on individual gliadin and glutenin protein levels are needed to determine how these environmental factors influence flour quality. Based on extraction and solubility properties, the gluten proteins can be separated into two major groups: the alcohol-soluble gliadins and the alcoholinsoluble glutenins [1]. The glutenins are classified as high molecular weight-glutenin subunits (HMW-GS) and low molecular weight-glutenin subunits (LMW-GS), which link together via intermolecular disulfide bonds to form large insoluble polymers. Variations in flour quality are related to genetic differences in gliadin and glutenin composition among wheat cultivars and to effects of environmental conditions on their relative proportions [2,3]

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