The control of abscission is an important agricultural concern because of its substantial effect
on crop yield and quality. Changes in gene expression are correlated with the ethylenemediated
execution of abscission. However, only few large-scale proteomic studies focused
on tomato pedicel abscission. Isobaric tag for relative and absolute quantification labeling
was used to examine the protein and phosphoprotein changes in the tomato pedicel AZ
(AZ) treated with ethylene or 1-methylcyclopropene. Among the 1429 quantified proteins,
383 unique peptides corresponding to 166 proteins showed higher than 1.5-fold change in
abundance. A total of 450 phosphopeptides were detected, among which 85 phosphopeptides
corresponding to 73 phosphoproteins were significantly regulated (>1.5-fold abundance
change) in response to ethylene. Protein and phosphoprotein sets showed 26 similar proteins.
Six phosphorylation motifs were extracted from the 138 phosphorylation sites. By analyzing
translational and modification levels, we found that the modification level was not due to
the translational changes. Comparison between the protein and phosphoprotein functions
revealed that the proteins acted mainly in the metabolic process and showed catalytic activity,
whereas most of the phosphoproteins showed signaling and transporting activities. Data
revealed the unique features of the AZ phosphoproteomics, thereby suggesting the involvement
of a complex network of kinase–substrate and phosphatas
The control of abscission is an important agricultural concern because of its substantial effect
on crop yield and quality. Changes in gene expression are correlated with the ethylenemediated
execution of abscission. However, only few large-scale proteomic studies focused
on tomato pedicel abscission. Isobaric tag for relative and absolute quantification labeling
was used to examine the protein and phosphoprotein changes in the tomato pedicel AZ
(AZ) treated with ethylene or 1-methylcyclopropene. Among the 1429 quantified proteins,
383 unique peptides corresponding to 166 proteins showed higher than 1.5-fold change in
abundance. A total of 450 phosphopeptides were detected, among which 85 phosphopeptides
corresponding to 73 phosphoproteins were significantly regulated (>1.5-fold abundance
change) in response to ethylene. Protein and phosphoprotein sets showed 26 similar proteins.
Six phosphorylation motifs were extracted from the 138 phosphorylation sites. By analyzing
translational and modification levels, we found that the modification level was not due to
the translational changes. Comparison between the protein and phosphoprotein functions
revealed that the proteins acted mainly in the metabolic process and showed catalytic activity,
whereas most of the phosphoproteins showed signaling and transporting activities. Data
revealed the unique features of the AZ phosphoproteomics, thereby suggesting the involvement
of a complex network of kinase–substrate and phosphatas
การแปล กรุณารอสักครู่..