Dataset Information

Large-scale phosphoproteome analysis in seedling leaves of Brachypodium distachyon L

ABSTRACT: In this study, we carried out the first large-scale phosphoproteome analysis of seedling leaves in Brachypodium accession Bd21 using TiO2 microcolumns combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS) and MaxQuant software. A total, 1,470 phosphorylation sites in 950 phosphoproteins were identified. Of the 950 phosphoproteins identified, 127 contained 3 to 8 phosphorylation sites. The phosphoproteins and phosphosites identified in our study expanded our knowledge of protein phosphorylation modification in plants, especially in monocot.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Brachypodium Distachyon (purple False Brome) (trachynia Distachya)

TISSUE(S): Plant Cell, Leaf

DISEASE(S): Disease Free

SUBMITTER: Dong-Wen Lv

LAB HEAD: Yue-Ming Yan

PROVIDER: PXD000868 | Pride | 2016-07-09

REPOSITORIES: Pride

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Large-scale phosphoproteome analysis in seedling leaves of Brachypodium distachyon L.

Lv Dong-Wen DW Lv Dong-Wen DW Li Xin X Zhang Ming M Gu Ai-Qin AQ Zhen Shou-Min SM Wang Chang C Li Xiao-Hui XH Yan Yue-Ming YM

BMC genomics 20140516

<h4>Background</h4>Protein phosphorylation is one of the most important post-translational modifications involved in the regulation of plant growth and development as well as diverse stress response. As a member of the Poaceae, Brachypodium distachyon L. is a new model plant for wheat and barley as well as several potential biofuel grasses such as switchgrass. Vegetative growth is vital for biomass accumulation of plants, but knowledge regarding the role of protein phosphorylation modification d ...[more]

PMID: 24885693

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