Large-Scale Comparative Phosphoproteomics Identifies Conserved Phosphorylation Sites in Plants

• Hirofumi Nakagami

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Naoyuki Sugiyama

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Keiichi Mochida

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Arsalan Daudi

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Yuko Yoshida

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Tetsuro Toyoda

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Masaru Tomita

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Yasushi Ishihama

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

• Ken Shirasu

  RIKEN Plant Science Center (H.N., K.M., A.D., K.S.) and RIKEN Bioinformatics and Systems Engineering Division (Y.Y., T.T.), Tsurumi-ku, Yokohama 230–0045, Japan; Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997–0017, Japan (N.S., M.T., Y.I.); PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102–0075, Japan (Y.I.)

抄録

Knowledge of phosphorylation events and their regulation is crucial to understand the functional biology of plants. Here, we report a large-scale phosphoproteome analysis in the model monocot rice (Oryza sativa  japonica ‘Nipponbare’), an economically important crop. Using unfractionated whole-cell lysates of rice cells, we identified 6,919 phosphopeptides from 3,393 proteins. To investigate the conservation of phosphoproteomes between plant species, we developed a novel phosphorylation-site evaluation method and performed a comparative analysis of rice and Arabidopsis (Arabidopsis thaliana). The ratio of tyrosine phosphorylation in the phosphoresidues of rice was equivalent to those in Arabidopsis and human. Furthermore, despite the phylogenetic distance and the use of different cell types, more than 50% of the phosphoproteins identified in rice and Arabidopsis, which possessed ortholog(s), had an orthologous phosphoprotein in the other species. Moreover, nearly half of the phosphorylated orthologous pairs were phosphorylated at equivalent sites. Further comparative analyses against the Medicago phosphoproteome also showed similar results. These data provide direct evidence for conserved regulatory mechanisms based on phosphorylation in plants. We also assessed the phosphorylation sites on nucleotide-binding leucine-rich repeat proteins and identified novel conserved phosphorylation sites that may regulate this class of proteins.

収録刊行物

• Plant Physiology

  Plant Physiology 153 (3), 1161-1174, 2010-05-13

  Oxford University Press (OUP)

キーワード

• Plant Science
• Genetics
• Physiology

詳細情報

• CRID: 1360002217846593152
• NII論文ID: 80021211314
• DOI: 10.1104/pp.110.157347
• ISSN: 15322548
• ISSN: http://id.crossref.org/issn/00320889
• Web Site: http://academic.oup.com/plphys/article-pdf/153/3/1161/38107616/plphys_v153_3_1161.pdf
• データソース種別:
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  • CiNii Articles
  • KAKEN