Abstract
BackgroundPhosphorylation modification, one of the most common post-translational modifications of proteins, widely participates in the regulation of plant growth and development. Fibers extracted from the stem bark of ramie are important natural textile fibers; however, the role of phosphorylation modification in the growth of ramie fibers is largely unknown.ResultsHere, we report a phosphoproteome analysis for the barks from the top and middle section of ramie stems, in which the fiber grows at different stages. A total of 10,320 phosphorylation sites from 9,170 unique phosphopeptides that were assigned to 3,506 proteins was identified, and 458 differentially phosphorylated sites from 323 proteins were detected in the fiber developmental barks. Twelve differentially phosphorylated proteins were the homologs of Arabidopsis fiber growth-related proteins. We further focused on the function of the differentially phosphorylated KNOX protein whole_GLEAN_10029667, and found that this protein dramatically repressed the fiber formation in Arabidopsis. Additionally, using a yeast two-hybridization assay, we identified a kinase and a phosphatase that interact with whole_GLEAN_10029667, indicating that they potentially target this KNOX protein to regulate its phosphorylation level.ConclusionThe finding of this study provided insights into the involvement of phosphorylation modification in ramie fiber growth, and our functional characterization of whole_GLEAN_10029667 provide the first evidence to indicate the involvement of phosphorylation modification in the regulation of KNOX protein function in plants.
Highlights
Phosphorylation modification, one of the most common post-translational modifications of proteins, widely participates in the regulation of plant growth and development
Characterization of the phosphoproteome of stem barks We carried out phosphoproteomic analyses for the top section of stems (TPS) and barks in the middle part of stem (MPS) of ramie bast barks using a UHPLC-MS/ MS system, and obtained 154,142 spectra (Table 1)
To gain an overview of the functions of proteins identified from the phosphoproteome, we carried out a prediction of their subcellular localization based on Gene Ontology (GO) annotation, and found that ~81.2% of the proteins were distributed in the chloroplast, cytoplasm, and/or nucleus (Fig. 1a)
Summary
Phosphorylation modification, one of the most common post-translational modifications of proteins, widely participates in the regulation of plant growth and development. Fibers extracted from the stem bark of ramie are important natural textile fibers; the role of phosphorylation modification in the growth of ramie fibers is largely unknown. Post-translational modifications (PTMs) have been identified as playing important roles in diverse biological processes, including gene expression, cell signaling, protein stabilization, and the activation/deactivation of enzymatic activity [1]. Ramie fibers, extracted from its stem bark, are among the most important raw materials in the production if industrial textiles. A large number of non-coding RNAs (ncRNAs) have been identified to play a potential role in the growth of ramie fiber [15, 16]. There has been little evidence to indicate the involvement of PTMs in the fiber growth of this crop
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