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Phosphoproteome analysis of Lotus japonicus seeds
Author(s) -
Ino Yoko,
Ishikawa Akiyo,
Nomura Ayako,
Kajiwara Hideyuki,
Harada Kyuya,
Hirano Hisashi
Publication year - 2014
Publication title -
proteomics
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201300237
Subject(s) - lotus japonicus , lotus , kinase , hypocotyl , cotyledon , biology , germination , microbiology and biotechnology , botany , biochemistry , gene , mutant
In this study, we report the first dataset of phosphoproteins of the seeds of a model plant, Lotus japonicus. This dataset might be useful in studying the regulatory mechanisms of seed germination in legume plants. By proteomic analysis of seeds following water absorption, we identified a total of 721 phosphopeptides derived from 343 phosphoproteins in cotyledons, and 931 phosphopeptides from 473 phosphoproteins in hypocotyls. Kinase-specific prediction analyses revealed that different kinases were activated in cotyledons and hypocotyls. In particular, many peptides containing ATM-kinase target motifs, X-X-pS/pT-Q-X-X, were detected in cotyledons. Moreover, by real-time RT-PCR analysis, we found that expression of a homolog of ATM kinase is upregulated specifically in cotyledons, suggesting that this ATM-kinase homolog plays a significant role in cell proliferation in the cotyledons of L. japonicus seeds. The data have been deposited to the ProteomeXchange with identifier PXD000053 (http://proteomecentral.proteomexchange.org/dataset/PXD000053).