Effect of Phosphorus Levels on the Protein Profiles of Secreted Protein and Root Surface Protein of Rice

• Published in: Journal of proteome research Vol. 12; no. 11; pp. 4748 - 4756
• Main Authors: Shinano, Takuro, Yoshimura, Tomoko, Watanabe, Toshihiro, Unno, Yusuke, Osaki, Mitsuru, Nanjo, Yohei, Komatsu, Setsuko
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 01.11.2013
• Subjects: Chromatography, Liquid; Culture Media - chemistry; Gene Expression Regulation, Plant - drug effects; Gene Expression Regulation, Plant - genetics; Oryza - drug effects; Oryza - genetics; Oryza - metabolism; Phosphorus - pharmacology; Plant Proteins - genetics; Plant Proteins - metabolism; Plant Roots - drug effects; Plant Roots - genetics; Proteomics - methods; Rhizosphere; Tandem Mass Spectrometry; root surface-binding protein; aseptic culture; Oryza saliva; phosphorus treatment; rhizosphere proteome; root secretory protein
• ISSN: 1535-3893; 1535-3907
• DOI: 10.1021/pr400614n

Plant roots are complicated organs that absorb water and nutrients from the soil. Roots also play an essential role in protecting plants from attack by soil pathogens and develop a beneficial role with some soil microorganisms. Plant-derived rhizosphere proteins (e.g., root secretory proteins and root surface binding proteins) are considered to play important roles in developing mutual relationships in the rhizosphere. In the rhizosphere, where plant roots meet the surrounding environment, it has been suggested that root secretory protein and root surface binding protein are important factors. Furthermore, it is not known how the physiological status of the plant affects the profile of these proteins. In this study, rice plants were grown aseptically, with or without phosphorus nutrition, and proteins were obtained from root bathing solution (designated as root secretory proteins) and obtained using 0.2 M CaCl2 solution (designated as root surface binding proteins). The total number of identified proteins in the root bathing solution was 458, and the number of root surface binding proteins was 256. More than half of the proteins were observed in both fractions. Most of the proteins were categorized as either having signal peptides or no membrane transport helix sites. The functional categorization suggested that most of the proteins seemed to have secretory pathways and were involved in defense/disease-related functions. These characteristics seem to be unique to rhizosphere proteins, and the latter might be part of the plants strategy to defeat pathogens in the soil. The low phosphorus treatment significantly increased the number of pathogenesis-related proteins in the root secretory proteins, whereas the change was small in the case of the root surface binding proteins. The results suggested that the roots are actively and selectively secreting protein into the rhizosphere.