Proteome study of the phloem sap of pumpkin using multidimensional protein identification technology
- Authors
- Cho, Won Kyong; Chen, Xiong-Yan; Rim, Yeonggil; Chu, Hyosub; Kim, Suwha; Kim, Seon-Won; Park, Zee-Yong; Kim, Jae-Yean
- Issue Date
- Jul-2010
- Publisher
- Elsevier BV
- Keywords
- Cucurbita maxima; Mass spectrometry; Phloem; Proteome; Pumpkin
- Citation
- Journal of Plant Physiology, v.167, no.10, pp 771 - 778
- Pages
- 8
- Indexed
- SCI
SCIE
SCOPUS
- Journal Title
- Journal of Plant Physiology
- Volume
- 167
- Number
- 10
- Start Page
- 771
- End Page
- 778
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/26055
- DOI
- 10.1016/j.jplph.2010.01.004
- ISSN
- 0176-1617
1618-1328
- Abstract
- The phloem is the major transport route for both small substances and large molecules, such as proteins and RNAs, from their sources to sink tissues. To investigate the proteins present in pumpkin phloem sap, proteome analysis using multidimensional protein identification technology was carried out. Pumpkin phloem peptides obtained by liquid chromatography/mass spectrometry/mass spectrometry were searched against pumpkin protein data derived from the National Center for Biotechnology Information. A total of 47 pumpkin phloem proteins were identified. The identified proteins mainly corresponded to enzymes involved in gibberellin biosynthesis, antioxidation processes, or defense mechanisms. Interestingly, seven enzymes required for gibberellin biosynthesis were identified for the first time by this proteomics approach. In summary, the new phloem proteins identified in this study provide strong evidence for stress and defense signaling and new insights regarding the role of gibberellin in the developmental programming of higher plants through the phloem. (C) 2010 Elsevier GmbH. All rights reserved.
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