Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grain

Wheat grain end-use value is determined by complex molecular interactions that occur during grain development, including those in the cell nucleus. However our knowledge of how the nuclear proteome changes during grain development is limited. Here, we analyzed nuclear proteins of developing wheat gr...

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Main Authors: Titouan eBonnot, Emmanuelle eBancel, Christophe eChambon, Julie eBoudet, Gérard eBranlard, Pierre eMartre
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-10-01
Series:Frontiers in Plant Science
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00905/full
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spelling doaj-e8c9dee8aa9d4f73b397a4c49243eca02020-11-24T20:44:15ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2015-10-01610.3389/fpls.2015.00905160382Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grainTitouan eBonnot0Titouan eBonnot1Emmanuelle eBancel2Emmanuelle eBancel3Christophe eChambon4Julie eBoudet5Julie eBoudet6Gérard eBranlard7Gérard eBranlard8Pierre eMartre9Pierre eMartre10Blaise Pascal UniversityINRABlaise Pascal UniversityINRAINRABlaise Pascal UniversityINRABlaise Pascal UniversityINRABlaise Pascal UniversityINRAWheat grain end-use value is determined by complex molecular interactions that occur during grain development, including those in the cell nucleus. However our knowledge of how the nuclear proteome changes during grain development is limited. Here, we analyzed nuclear proteins of developing wheat grains collected during the cellularization, effective grain-filling and maturation phases of development, respectively. Nuclear proteins were extracted and separated by two-dimensional gel electrophoresis. Image analysis revealed 371 and 299 reproducible spots in gels with first dimension separation along pH 4-7 and pH 6-11 isoelectric gradients, respectively. The relative abundance of 464 (67%) protein spots changed during grain development. Abundance profiles of these proteins clustered in six groups associated with the major phases and phase transitions of grain development. Using nano liquid chromatography-tandem mass spectrometry to analyse 387 variant and non-variant protein spots, 114 different proteins were identified that were classified into 16 functional classes. We noted that some proteins involved in the regulation of transcription, like HMG1/2-like protein and histone deacetylase HDAC2, were most abundant before the phase transition from cellularization to grain-filling, suggesting that major transcriptional changes occur during this key developmental phase. The maturation period was characterized by high relative abundance of proteins involved in ribosome biogenesis. Data are available via ProteomeXchange with identifier PXD002999.http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00905/fullNuclear ProteinsLC-MS/MSwheat2D gel electrophoresisDeveloping grain
collection DOAJ
language English
format Article
sources DOAJ
author Titouan eBonnot
Titouan eBonnot
Emmanuelle eBancel
Emmanuelle eBancel
Christophe eChambon
Julie eBoudet
Julie eBoudet
Gérard eBranlard
Gérard eBranlard
Pierre eMartre
Pierre eMartre
spellingShingle Titouan eBonnot
Titouan eBonnot
Emmanuelle eBancel
Emmanuelle eBancel
Christophe eChambon
Julie eBoudet
Julie eBoudet
Gérard eBranlard
Gérard eBranlard
Pierre eMartre
Pierre eMartre
Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grain
Frontiers in Plant Science
Nuclear Proteins
LC-MS/MS
wheat
2D gel electrophoresis
Developing grain
author_facet Titouan eBonnot
Titouan eBonnot
Emmanuelle eBancel
Emmanuelle eBancel
Christophe eChambon
Julie eBoudet
Julie eBoudet
Gérard eBranlard
Gérard eBranlard
Pierre eMartre
Pierre eMartre
author_sort Titouan eBonnot
title Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grain
title_short Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grain
title_full Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grain
title_fullStr Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grain
title_full_unstemmed Changes in the nuclear proteome of developing wheat (Triticum aestivum L.) grain
title_sort changes in the nuclear proteome of developing wheat (triticum aestivum l.) grain
publisher Frontiers Media S.A.
series Frontiers in Plant Science
issn 1664-462X
publishDate 2015-10-01
description Wheat grain end-use value is determined by complex molecular interactions that occur during grain development, including those in the cell nucleus. However our knowledge of how the nuclear proteome changes during grain development is limited. Here, we analyzed nuclear proteins of developing wheat grains collected during the cellularization, effective grain-filling and maturation phases of development, respectively. Nuclear proteins were extracted and separated by two-dimensional gel electrophoresis. Image analysis revealed 371 and 299 reproducible spots in gels with first dimension separation along pH 4-7 and pH 6-11 isoelectric gradients, respectively. The relative abundance of 464 (67%) protein spots changed during grain development. Abundance profiles of these proteins clustered in six groups associated with the major phases and phase transitions of grain development. Using nano liquid chromatography-tandem mass spectrometry to analyse 387 variant and non-variant protein spots, 114 different proteins were identified that were classified into 16 functional classes. We noted that some proteins involved in the regulation of transcription, like HMG1/2-like protein and histone deacetylase HDAC2, were most abundant before the phase transition from cellularization to grain-filling, suggesting that major transcriptional changes occur during this key developmental phase. The maturation period was characterized by high relative abundance of proteins involved in ribosome biogenesis. Data are available via ProteomeXchange with identifier PXD002999.
topic Nuclear Proteins
LC-MS/MS
wheat
2D gel electrophoresis
Developing grain
url http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00905/full
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