Large-scale analysis of phosphorylated proteins in maize leaf

Phosphorylation is an ubiquitous regulatory mechanism governing the activity, subcellular localization, and intermolecular interactions of proteins. To identify a broad range of phosphoproteins from Zea mays, we enriched phosphopeptides from Zea mays leaves using titanium dioxide microcolumns and th...

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Bibliographic Details
Published in:Planta 2011-02, Vol.233 (2), p.383-392
Main Authors: Bi, Ying-Dong, Wang, Hong-Xia, Lu, Tian-Cong, Li, Xiao-hui, Shen, Zhuo, Chen, Yi-Bo, Wang, Bai-Chen
Format: Article
Language:English
Subjects:
Agriculture
Biological and medical sciences
Biomedical and Life Sciences
Carbohydrate metabolism
Chromatin - metabolism
Corn
DNA, Plant - metabolism
Ecology
Forestry
Fundamental and applied biological sciences. Psychology
Gene Expression Profiling
Gene expression regulation
Gene Expression Regulation, Plant - physiology
Life Sciences
NanoLC-MS/MS
Original Article
Phosphoproteins
Phosphorylation
Plant Leaves - metabolism
Plant Proteins - genetics
Plant Proteins - metabolism
Plant Sciences
Protein metabolism
Proteins
Proteomics
RNA
RNA, Plant - metabolism
Splicing
Transcription Factors - genetics
Transcription Factors - metabolism
Zea mays - genetics
Zea mays - metabolism
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Summary:Phosphorylation is an ubiquitous regulatory mechanism governing the activity, subcellular localization, and intermolecular interactions of proteins. To identify a broad range of phosphoproteins from Zea mays, we enriched phosphopeptides from Zea mays leaves using titanium dioxide microcolumns and then extensively fractionated and identified the phosphopeptides by mass spectrometry. A total of 165 unique phosphorylation sites with a putative role in biological processes were identified in 125 phosphoproteins. Most of these proteins are involved in metabolism, including carbohydrate and protein metabolism. We identified novel phosphorylation sites on translation initiation factors, splicing factors, nucleolar RNA helicases, and chromatin-remodeling proteins such as histone deacetylases. Intriguingly, we also identified phosphorylation sites on several proteins associated with photosynthesis, and we speculate that these sites may be involved in carbohydrate metabolism or electron transport. Among these phosphoproteins, phosphoenolpyruvate carboxylase and NADH: nitrate reductase (NR) which catalyzes the rate-limiting and regulated step in the pathway of inorganic nitrogen assimilation were identified. A conserved phosphorylation site was found in the cytochrome b5 heme-binding domain of NADH: nitrate reductase, suggesting that NADH: nitrate reductase is phosphorylated by the same protein kinase or highly related kinases. These data demonstrate that the pathways that regulate diverse processes in plants are major targets of phosphorylation.
ISSN:0032-0935
1432-2048
DOI:10.1007/s00425-010-1291-x