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Cited 18 time in webofscience Cited 21 time in scopus
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Proteome study of the phloem sap of pumpkin using multidimensional protein identification technology

Authors
Cho, Won KyongChen, Xiong-YanRim, YeonggilChu, HyosubKim, SuwhaKim, Seon-WonPark, Zee-YongKim, 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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