title: Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar.
abstract: BACKGROUND
  Although there has been considerable progress made towards understanding the molecular mechanisms of bud dormancy, the roles of protein phosphorylation in the process of dormancy regulation in woody plants remain unclear.
  
  
  RESULTS
  We used mass spectrometry combined with TiO₂ phosphopeptide-enrichment strategies to investigate the phosphoproteome of dormant terminal buds (DTBs) in poplar (Populus simonii × P. nigra). There were 161 unique phosphorylated sites in 161 phosphopeptides from 151 proteins; 141 proteins have orthologs in Arabidopsis, and 10 proteins are unique to poplar. Only 34 sites in proteins in poplar did not match well with the equivalent phosphorylation sites of their orthologs in Arabidopsis, indicating that regulatory mechanisms are well conserved between poplar and Arabidopsis. Further functional classifications showed that most of these phosphoproteins were involved in binding and catalytic activity. Extraction of the phosphorylation motif using Motif-X indicated that proline-directed kinases are a major kinase group involved in protein phosphorylation in dormant poplar tissues.
  
  
  CONCLUSIONS
  This study provides evidence about the significance of protein phosphorylation during dormancy, and will be useful for similar studies on other woody plants.
authors.affiliation: State Key Laboratory of Forest Genetics and Tree Breeding (Northeast Forestry University), 26 Hexing Road, Harbin 150040, China.
authors.forename: Chang-Cai
authors.initials: CC
authors.lastname: Liu
authors.forename: Chang-Fu
authors.initials: CF
authors.lastname: Liu
authors.forename: Hong-Xia
authors.initials: HX
authors.lastname: Wang
authors.forename: Zhi-Ying
authors.initials: ZY
authors.lastname: Shen
authors.forename: Chuan-Ping
authors.initials: CP
authors.lastname: Yang
authors.forename: Zhi-Gang
authors.initials: ZG
authors.lastname: Wei
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry / Q000502:physiology; D029681:Arabidopsis Proteins / Q000737:chemistry; D017124:Conserved Sequence; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010940:Plant Proteins / Q000737:chemistry*; D018520:Plant Shoots / Q000737:chemistry / Q000502:physiology*; D032107:Populus / Q000737:chemistry / Q000502:physiology*; D011494:Protein Kinases / Q000502:physiology; D020543:Proteome / Q000032:analysis*; D015398:Signal Transduction
chemical_list: D029681:Arabidopsis Proteins; D010940:Plant Proteins; D020543:Proteome; D011494:Protein Kinases
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