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Proteomic analysis of the secretome of rice calli
Author(s) -
Cho Won Kyong,
Chen Xiong Yan,
Chu Hyosub,
Rim Yeonggil,
Kim Suwha,
Kim Sun Tae,
Kim SeonWon,
Park ZeeYong,
Kim JaeYean
Publication year - 2009
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.2008.01198.x
Subject(s) - secretory protein , proteome , arabidopsis , proteomics , biology , signal peptide , biogenesis , microbiology and biotechnology , secretion , cell wall , biochemistry , secretory pathway , cell , gene , peptide sequence , mutant , golgi apparatus
The cell wall and extracellular matrix in higher plants include secreted proteins that play critical roles in a wide range of cellular processes, such as structural integrity and biogenesis. Compared with the intensive cell wall proteomic studies in Arabidopsis , the list of cell wall proteins identified in monocot species is lacking. Therefore, we conducted a large‐scale proteomic analysis of secreted proteins from rice. Highly purified secreted rice proteins were obtained from the medium of a suspension of callus culture and were analyzed with multidimensional protein identification technology (MudPIT). As a result, we could detect a total of 555 rice proteins by MudPIT analysis. Based on bioinformatic analyses, 27.7% (154 proteins) of the identified proteins are considered to be secreted proteins because they possess a signal peptide for the secretory pathway. Among the 154 identified proteins, 27% were functionally categorized as stress response proteins, followed by metabolic proteins (26%) and factors involved in protein modification (24%). Comparative analysis of cell wall proteins from Arabidopsis and rice revealed that one third of the secreted rice proteins overlapped with those of Arabidopsis . Furthermore, 25 novel rice‐specific secreted proteins were found. This work presents the large scale of the rice secretory proteome from culture medium, which contributes to a deeper understanding of the rice secretome.