Proteomic and phosphoproteomic analyses reveal extensive phosphorylation of regulatory proteins in developing rice anthers. (10th October 2015)
- Record Type:
- Journal Article
- Title:
- Proteomic and phosphoproteomic analyses reveal extensive phosphorylation of regulatory proteins in developing rice anthers. (10th October 2015)
- Main Title:
- Proteomic and phosphoproteomic analyses reveal extensive phosphorylation of regulatory proteins in developing rice anthers
- Authors:
- Ye, Juanying
Zhang, Zaibao
Long, Haifei
Zhang, Zhimin
Hong, Yue
Zhang, Xumin
You, Chenjiang
Liang, Wanqi
Ma, Hong
Lu, Pingli - Abstract:
- <abstract abstract-type="main" id="tpj13019-abs-0001"> <title>Summary</title> <p>Anther development, particularly around the time of meiosis, is extremely crucial for plant sexual reproduction. Meanwhile, cell‐to‐cell communication between somatic (especial tapetum) cells and meiocytes are important for both somatic anther development and meiosis. To investigate possible molecular mechanisms modulating protein activities during anther development, we applied high‐resolution mass spectrometry‐based proteomic and phosphoproteomic analyses for developing <underline>r</underline>ice (<italic>Oryza sativa</italic>) <underline>a</underline>nthers around the time of <underline>m</underline>eiosis (RAM). In total, we identified 4984 proteins and 3203 phosphoproteins with 8973 unique phosphorylation sites (p‐sites). Among those detected here, 1544 phosphoproteins are currently absent in the Plant Protein Phosphorylation DataBase (P<sup>3</sup>DB), substantially enriching plant phosphorylation information. Mapman enrichment analysis showed that 'DNA repair', 'transcription regulation' and 'signaling' related proteins were overrepresented in the phosphorylated proteins. Ten genetically identified rice meiotic proteins were detected to be phosphorylated at a total of 25 p‐sites; moreover more than 400 meiotically expressed proteins were revealed to be phosphorylated and their phosphorylation sites were precisely assigned. 163 putative secretory proteins, possibly functioning in<abstract abstract-type="main" id="tpj13019-abs-0001"> <title>Summary</title> <p>Anther development, particularly around the time of meiosis, is extremely crucial for plant sexual reproduction. Meanwhile, cell‐to‐cell communication between somatic (especial tapetum) cells and meiocytes are important for both somatic anther development and meiosis. To investigate possible molecular mechanisms modulating protein activities during anther development, we applied high‐resolution mass spectrometry‐based proteomic and phosphoproteomic analyses for developing <underline>r</underline>ice (<italic>Oryza sativa</italic>) <underline>a</underline>nthers around the time of <underline>m</underline>eiosis (RAM). In total, we identified 4984 proteins and 3203 phosphoproteins with 8973 unique phosphorylation sites (p‐sites). Among those detected here, 1544 phosphoproteins are currently absent in the Plant Protein Phosphorylation DataBase (P<sup>3</sup>DB), substantially enriching plant phosphorylation information. Mapman enrichment analysis showed that 'DNA repair', 'transcription regulation' and 'signaling' related proteins were overrepresented in the phosphorylated proteins. Ten genetically identified rice meiotic proteins were detected to be phosphorylated at a total of 25 p‐sites; moreover more than 400 meiotically expressed proteins were revealed to be phosphorylated and their phosphorylation sites were precisely assigned. 163 putative secretory proteins, possibly functioning in cell‐to‐cell communication, are also phosphorylated. Furthermore, we showed that DNA synthesis, RNA splicing and RNA‐directed DNA methylation pathways are extensively affected by phosphorylation. In addition, our data support 46 kinase‐substrate pairs predicted by the rice Kinase‐Protein Interaction Map, with SnRK1 substrates highly enriched. Taken together, our data revealed extensive protein phosphorylation during anther development, suggesting an important post‐translational modification affecting protein activity.</p> </abstract> … (more)
- Is Part Of:
- Plant journal. Volume 84:Number 3(2015:Nov.)
- Journal:
- Plant journal
- Issue:
- Volume 84:Number 3(2015:Nov.)
- Issue Display:
- Volume 84, Issue 3 (2015)
- Year:
- 2015
- Volume:
- 84
- Issue:
- 3
- Issue Sort Value:
- 2015-0084-0003-0000
- Page Start:
- 527
- Page End:
- 544
- Publication Date:
- 2015-10-10
- Subjects:
- Plant molecular biology -- Periodicals
Plant cells and tissues -- Periodicals
Botany -- Periodicals
580 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-313X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/tpj.13019 ↗
- Languages:
- English
- ISSNs:
- 0960-7412
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6519.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4156.xml