Phosphoproteomic analysis of chromoplasts from sweet orange during fruit ripening.
Identifieur interne : 000976 ( Main/Merge ); précédent : 000975; suivant : 000977Phosphoproteomic analysis of chromoplasts from sweet orange during fruit ripening.
Auteurs : Yunliu Zeng [République populaire de Chine] ; Zhiyong Pan ; Lun Wang ; Yuduan Ding ; Qiang Xu ; Shunyuan Xiao ; Xiuxin DengSource :
- Physiologia plantarum [ 1399-3054 ] ; 2014.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Arabidopsis (metabolism), Chromatography, Liquid, Citrus sinensis (growth & development), Citrus sinensis (metabolism), Conserved Sequence, Energy Metabolism, Fruit (growth & development), Fruit (metabolism), Homeostasis, Metabolic Networks and Pathways, Molecular Sequence Data, Peptides (chemistry), Peptides (metabolism), Phosphoproteins (chemistry), Phosphoproteins (classification), Phosphoproteins (metabolism), Phosphorylation, Plant Proteins (chemistry), Plant Proteins (metabolism), Plastids (metabolism), Proteome (chemistry), Proteome (metabolism), Proteomics (methods).
- MESH :
- chemical , chemistry : Peptides, Phosphoproteins, Plant Proteins, Proteome.
- chemical , classification : Phosphoproteins.
- growth & development : Citrus sinensis, Fruit.
- metabolism : Arabidopsis, Citrus sinensis, Fruit, Peptides, Phosphoproteins, Plant Proteins, Plastids, Proteome.
- methods : Proteomics.
- Amino Acid Motifs, Amino Acid Sequence, Chromatography, Liquid, Conserved Sequence, Energy Metabolism, Homeostasis, Metabolic Networks and Pathways, Molecular Sequence Data, Phosphorylation.
Abstract
Like other types of plastids, chromoplasts have essential biosynthetic and metabolic activities which may be regulated via post-translational modifications, such as phosphorylation, of their resident proteins. We here report a proteome-wide mapping of in vivo phosphorylation sites in chromoplast-enriched samples prepared from sweet orange [Citrus sinensis (L.) Osbeck] at different ripening stages by titanium dioxide-based affinity chromatography for phosphoprotein enrichment with LC-MS/MS. A total of 109 plastid-localized phosphoprotein candidates were identified that correspond to 179 unique phosphorylation sites in 135 phosphopeptides. On the basis of Motif-X analysis, two distinct types of phosphorylation sites, one as proline-directed phosphorylation motif and the other as casein kinase II motif, can be generalized from these identified phosphopeptides. While most identified phosphoproteins show high homology to those already identified in plastids, approximately 22% of them are novel based on BLAST search using the public databases PhosPhAt and P(3) DB. A close comparative analysis showed that approximately 50% of the phosphoproteins identified in citrus chromoplasts find obvious counterparts in the chloroplast phosphoproteome, suggesting a rather high-level of conservation in basic metabolic activities in these two types of plastids. Not surprisingly, the phosphoproteome of citrus chromoplasts is also characterized by the lack of phosphoproteins involved in photosynthesis and by the presence of more phosphoproteins implicated in stress/redox responses. This study presents the first comprehensive phosphoproteomic analysis of chromoplasts and may help to understand how phosphorylation regulates differentiation of citrus chromoplasts during fruit ripening.
DOI: 10.1111/ppl.12080
PubMed: 23786612
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<term>Energy Metabolism</term>
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<front><div type="abstract" xml:lang="en">Like other types of plastids, chromoplasts have essential biosynthetic and metabolic activities which may be regulated via post-translational modifications, such as phosphorylation, of their resident proteins. We here report a proteome-wide mapping of in vivo phosphorylation sites in chromoplast-enriched samples prepared from sweet orange [Citrus sinensis (L.) Osbeck] at different ripening stages by titanium dioxide-based affinity chromatography for phosphoprotein enrichment with LC-MS/MS. A total of 109 plastid-localized phosphoprotein candidates were identified that correspond to 179 unique phosphorylation sites in 135 phosphopeptides. On the basis of Motif-X analysis, two distinct types of phosphorylation sites, one as proline-directed phosphorylation motif and the other as casein kinase II motif, can be generalized from these identified phosphopeptides. While most identified phosphoproteins show high homology to those already identified in plastids, approximately 22% of them are novel based on BLAST search using the public databases PhosPhAt and P(3) DB. A close comparative analysis showed that approximately 50% of the phosphoproteins identified in citrus chromoplasts find obvious counterparts in the chloroplast phosphoproteome, suggesting a rather high-level of conservation in basic metabolic activities in these two types of plastids. Not surprisingly, the phosphoproteome of citrus chromoplasts is also characterized by the lack of phosphoproteins involved in photosynthesis and by the presence of more phosphoproteins implicated in stress/redox responses. This study presents the first comprehensive phosphoproteomic analysis of chromoplasts and may help to understand how phosphorylation regulates differentiation of citrus chromoplasts during fruit ripening.</div>
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