Quantitative phosphoproteomic analysis of early seed development in rice (Oryza sativa L.)

Quantitative phosphoproteomic analysis of early seed development in rice (Oryza sativa L.) Rice (Oryza sativa L.) seed serves as a major food source for over half of the global population. Though it has been long recognized that phosphorylation plays an essential role in rice seed development, the phosphorylation events and dynamics in this process remain largely unknown so far. Here, we report the first large scale identification of rice seed phosphoproteins and phosphosites by using a quantitative phosphoproteomic approach. Thorough proteomic studies in pistils and seeds at 3, 7 days after pollination resulted in the successful identification of 3885, 4313 and 4135 phosphopeptides respectively. A total of 2487 proteins were differentially phosphorylated among the three stages, including Kip related protein 1, Rice basic leucine zipper factor 1, Rice prolamin box binding factor and numerous other master regulators of rice seed development. Moreover, differentially phosphorylated proteins may be extensively involved in the biosynthesis and signaling pathways of phytohormones such as auxin, gibberellin, abscisic acid and brassinosteroid. Our results strongly indicated that protein phosphorylation is a key mechanism regulating cell proliferation and enlargement, phytohormone biosynthesis and signaling, grain filling and grain quality during rice seed development. Overall, the current study enhanced our understanding of the rice phosphoproteome and shed novel insight into the regulatory mechanism of rice seed development. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Quantitative phosphoproteomic analysis of early seed development in rice (Oryza sativa L.)

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Publisher
Springer Netherlands
Copyright
Copyright © 2015 by Springer Science+Business Media Dordrecht
Subject
Life Sciences; Plant Sciences; Biochemistry, general; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1007/s11103-015-0410-2
Publisher site
See Article on Publisher Site

Abstract

Rice (Oryza sativa L.) seed serves as a major food source for over half of the global population. Though it has been long recognized that phosphorylation plays an essential role in rice seed development, the phosphorylation events and dynamics in this process remain largely unknown so far. Here, we report the first large scale identification of rice seed phosphoproteins and phosphosites by using a quantitative phosphoproteomic approach. Thorough proteomic studies in pistils and seeds at 3, 7 days after pollination resulted in the successful identification of 3885, 4313 and 4135 phosphopeptides respectively. A total of 2487 proteins were differentially phosphorylated among the three stages, including Kip related protein 1, Rice basic leucine zipper factor 1, Rice prolamin box binding factor and numerous other master regulators of rice seed development. Moreover, differentially phosphorylated proteins may be extensively involved in the biosynthesis and signaling pathways of phytohormones such as auxin, gibberellin, abscisic acid and brassinosteroid. Our results strongly indicated that protein phosphorylation is a key mechanism regulating cell proliferation and enlargement, phytohormone biosynthesis and signaling, grain filling and grain quality during rice seed development. Overall, the current study enhanced our understanding of the rice phosphoproteome and shed novel insight into the regulatory mechanism of rice seed development.

Journal

Plant Molecular BiologySpringer Journals

Published: Nov 28, 2015

References

  • The cyclin-dependent kinase inhibitor Orysa; KRP1 plays an important role in seed development of rice
    Barroco, RM; Peres, A; Droual, AM; Veylder, L; Nguyen, SL; Wolf, J; Mironov, V; Peerbolte, R; Beemster, GT; Inze, D; Broekaert, WF; Frankard, V
  • Abscisic acid: emergence of a core signaling network
    Cutler, SR; Rodriguez, PL; Finkelstein, RR; Abrams, SR
  • Use of proteomics to understand seed development in rice
    Deng, ZY; Gong, CY; Wang, T
  • SMALL GRAIN 1, which encodes a mitogen-activated protein kinase kinase 4, influences grain size in rice
    Duan, P; Rao, Y; Zeng, D; Yang, Y; Xu, R; Zhang, B; Dong, G; Qian, Q; Li, Y
  • The rice cyclin-dependent kinase-activating kinase R2 regulates S-phase progression
    Fabian-Marwedel, T; Umeda, M; Sauter, M
  • GID2, an F-box subunit of the SCF E3 complex, specifically interacts with phosphorylated SLR1 protein and regulates the gibberellin-dependent degradation of SLR1 in rice
    Gomi, K; Sasaki, A; Itoh, H; Ueguchi-Tanaka, M; Ashikari, M; Kitano, H; Matsuoka, M

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