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Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar.

Identifieur interne : 002E34 ( Main/Exploration ); précédent : 002E33; suivant : 002E35

Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar.

Auteurs : Chang-Cai Liu [République populaire de Chine] ; Chang-Fu Liu ; Hong-Xia Wang ; Zhi-Ying Shen ; Chuan-Ping Yang ; Zhi-Gang Wei

Source :

RBID : pubmed:22074553

Descripteurs français

English descriptors

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.


DOI: 10.1186/1471-2229-11-158
PubMed: 22074553
PubMed Central: PMC3234192


Affiliations:


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Le document en format XML

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<b>BACKGROUND</b>
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<p>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.</p>
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<b>RESULTS</b>
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<p>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.</p>
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