Phosphoproteome analysis of Lotus japonicus seeds

Proteomics. 2014 Jan;14(1):116-20. doi: 10.1002/pmic.201300237.

Abstract

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).

Keywords: Legume; Lotus japonicus; MS; Phosphoprotein; Plant proteomics.

MeSH terms

  • Cotyledon / chemistry
  • Hypocotyl / chemistry
  • Lotus / chemistry*
  • Mass Spectrometry
  • Peptide Fragments / analysis
  • Peptide Fragments / chemistry
  • Phosphoproteins / analysis*
  • Phosphoproteins / chemistry
  • Plant Proteins / analysis*
  • Plant Proteins / chemistry
  • Proteome / analysis*
  • Proteome / chemistry
  • Proteomics / methods
  • Seeds / chemistry*

Substances

  • Peptide Fragments
  • Phosphoproteins
  • Plant Proteins
  • Proteome