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A phosphoproteomic landscape of rice (Oryza sativa L.) tissues

ABSTRACT: Here, we first reported the construction of a phosphoproteomic landscape of 6 tissues, including callus, leaves, roots, shoot meristem (SM), young panicles (YP) and mature panicles (MP), from Nipponbare (Oryza sativa ssp. japonica). By employing a non-gel, quantitative phosphoproteomic approach, a total of 4792 phosphopeptides from 2657 phosphoproteins were identified, which were found to be differentially phosphorylated among tissues.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Oryza Sativa (rice)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Jian Zhang

LAB HEAD: Jian Zhang

PROVIDER: PXD005241 | Pride | 2018-04-11

REPOSITORIES: Pride

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			Action	DRS
	Rice_phos_callus_TiO2_25per_F1_R1.raw.raw	Raw
	Rice_phos_callus_TiO2_25per_F2_R1.raw.raw	Raw
	Rice_phos_callus_TiO2_25per_F3_R1.raw.raw	Raw
	Rice_phos_callus_TiO2_25per_peptide.xlsx	Xlsx
	Rice_phos_callus_TiO2_25per_protein.xlsx	Xlsx

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Publications

A phosphoproteomic landscape of rice (Oryza sativa) tissues.

Wang Yifeng Y Tong Xiaohong X Qiu Jiehua J Li Zhiyong Z Zhao Juan J Hou Yuxuan Y Tang Liqun L Zhang Jian J

Physiologia plantarum 20170525 4

Protein phosphorylation is an important posttranslational modification that regulates various plant developmental processes. Here, we report a comprehensive, quantitative phosphoproteomic profile of six rice tissues, including callus, leaf, root, shoot meristem, young panicle and mature panicle from Nipponbare by employing a mass spectrometry (MS)-based, label-free approach. A total of 7171 unique phosphorylation sites in 4792 phosphopeptides from 2657 phosphoproteins were identified, of which 4 ...[more]

PMID: 28382632

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