Dynamic proteomic profile of potato tuber during its in vitro development = 감자 기내소괴경 발달과정의 프로테움 프로파일

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Title
Dynamic proteomic profile of potato tuber during its in vitro development = 감자 기내소괴경 발달과정의 프로테움 프로파일
Author(s)
J W Yu; J S Choi; C P Upadhyaya; S O Kwon; M A Gururani; A Nookaraju; J H Nam; C W Choi; S I Kim; H Ajappala; Hyun Soon KimJae Heung Jeon; S W Park
Bibliographic Citation
Plant Science, vol. 195, no. 1, pp. 1-9
Publication Year
2012
Abstract
Potato tuberization is a complicated biochemical process, which is dependent on external environmental factors. Tuber development in potato consists of a series of biochemical and morphological processes at the stolon tip. Signal transduction proteins are involved in the source-sink transition during potato tuberization. In the present study, we examined protein profiles under in vitro tuber-inducing conditions using a shotgun proteomic approach involving denaturing gel electrophoresis and liquid chromatography-mass spectrometry. A total of 251 proteins were identified and classified into 9 groups according to distinctive expression patterns during the tuberization stage. Stolon stage-specific proteins were primarily involved in the photosynthetic machinery. Proteins specific to the initial tuber stage included patatin. Proteins specific to the developing tuber stage included 6-fructokinase, phytoalexin-deficient 4-1, metallothionein II-like protein, and malate dehydrogenase. Novel stage-specific proteins identified during in vitro tuberization were ferredoxin-NADP reductase, 34. kDa porin, aquaporin, calmodulin, ripening-regulated protein, and starch synthase. Superoxide dismutase, dehydroascorbate reductase, and catalase I were most abundantly expressed in the stolon; however, the enzyme activities of these proteins were most activated at the initial tuber. The present shotgun proteomic study provides insights into the proteins that show altered expression during in vitro potato tuberization.
Keyword
Potato tuberShotgun proteomicsStage-specific proteinTuberization
ISSN
0168-9452
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.plantsci.2012.06.007
Type
Article
Appears in Collections:
Division of Biomaterials Research > Plant Systems Engineering Research > 1. Journal Articles
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