Developmental changes in the metabolic protein profiles of wheat endosperm

Abstract

A combined two-dimensional gel electrophoresis-mass spectrometry approach was utilized to identify over 250 proteins of wheat (Triticum aestivum L., cv. Butte 86) starchy endosperm that participate in 13 biochemical processes: ATP interconversion reactions, carbohydrate metabolism, cell division, cytoskeleton, lipid metabolism, nitrogen metabolism, protein synthesis/assembly, protein turnover, signal transduction, protein storage, stress/defense, transcription/translation, and transport. Endosperm protein populations were compared at early (10 days post-anthesis, dpa) and late (36 dpa) stages of grain development. Analysis of protein number and spot volume revealed that carbohydrate metabolism, transcription/translation, and protein synthesis/assembly were the principal endosperm functions at 10 dpa followed by nitrogen metabolism, protein turnover, cytoskeleton, cell division, signal transduction, and lipid metabolism. Carbohydrate metabolism and protein synthesis/assembly were also major functions at 36 dpa, but stress/defense and storage were predominant. The results provide insight into biochemical events taking place during wheat grain development and highlight the value of proteomics in characterizing complex biochemical processes. Further, the proteome maps will facilitate future studies addressing the effects of genetic and environmental factors on the development and quality of wheat grain.

Two-dimensional gel electrophoretic protein profile analysis during seed development of Ocotea catharinensis: a recalcitrant seed species

“…A decrease in the number of proteins with low molecular weight and an increase in those with high molecular weight, during seed development were evident. An increase in high molecular weight protein expression is fundamental for embryo development, as they are related to maintenance activities and storage, whereas low-weight proteins are mainly related to synthesis (Vensel et al 2005).…”

Coping with Wheat Quality in a Changing Environment: Proteomics Evidence for Stress Caused by Environmental Changes

“…Whatever the cultivar studied, high temperatures have been shown to shorten the effective grain fi lling period, and may signifi cantly increase protein concentration because of more dramatic effect on starch than on protein accumulation Blumenthal et al 1991aBlumenthal et al , b , 1995Corbellini et al 1998 ;Triboï et al 2003 ). Many studies have addressed the responses of wheat grain to high temperatures during grain fi lling using either transcriptomics tools (Altenbach and Kothari 2004 ;Altenbach et al 2007 ;Hurkman et al 2003 ;Perrotta et al 1998 ) or proteomics approaches (Hurkman et al 2009 ;Laino et al 2010 ;Majoul et al 2003Majoul et al , 2004Majoul-Haddad et al 2013 ;Skylas et al 2002 ;Vensel et al 2005 ). In the present study, major events occurring in the wheat endosperm in response to high temperatures during grain fi lling were investigated using proteomics approaches.…”

Variant high-molecular-weight glutenin subunits arising from biolistic transformation of wheat

“…Identification of protein-containing bands was carried out as previously described (Vensel et al, 2005). The 96-well collection plate from the DigestPro was inserted into the autosampler of the Reverse-Phase (RP)-HPLC system that was interfaced to a QSTAR PULSAR i quadrupole time-of-flight mass spectrometer (Applied Biosystems/MDS Sciex, Toronto, CA).…”

“…The 96-well collection plate from the DigestPro was inserted into the autosampler of the Reverse-Phase (RP)-HPLC system that was interfaced to a QSTAR PULSAR i quadrupole time-of-flight mass spectrometer (Applied Biosystems/MDS Sciex, Toronto, CA). Conditions for operation of the instrument were as previously described (Vensel et al, 2005). A minimum of four independent samples for each protein variant were excised from gels and analyzed.…”