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고려인삼의 건조 스트레스 처리에 따른 단백질체 비표지 정량분석
정주용(Ju Young Jung),민철우(Cheol Woo Min),신혜원(Hye Won Shin),Truong Van Nguyen,김지현(Ji hyun Kim),김의정(Eui Jung Kim),조익현(Ick Hyun Jo),김유진(Yu Jin Kim),김선태(Sun Tae Kim) 한국약용작물학회 2021 한국약용작물학회지 Vol.29 No.6
Background: Korean ginseng (Panax ginseng Meyer) has long been cultivated as an important medicinal plant. Moderate water loss resulting form drought stress can impairs the growth of ginseng and lead to yield reduction. However, the mechanisms by which drought stress affects ginseng at the proteome level remain pooly undersood. Methods and Results: We carried out label-free quantitative proteomic analysis of ginseng roots subjected to drought stress (grown at less than 10% soil moisture for 2 weeks) and, compared the results with a control samples of ginseng grown at 25% soil moisture. The analysis was carried out using liquid chromatography with tandem mass spectrometry. A total of 2,471 proteins were identified, and 195 of which showed significant modulation. Functional classification revealed that proteins involved in calcium signaling, and photosynthesis and, production of secondary metabolites were enriched in the control sample (cluster_1), whereas proteins associated with stress response redox reaction, electron transport, and protein synthesis were enriched in the drought-stressed root (cluster_2). Conclusions: Our results provide an overview of drought-induced proteomic changes in ginseng root, and illuminate their correlation with physiological changes, revealing potential proteomic markers of drought stress in ginseng.
벼의 차세대 단백질체 분석을 위한 질량분석기 호환의 광분해성 계면활성제의 적용
신혜원(Hye Won Shin),응웬반쯔엉(Truong Van Nguyen),정주용(Ju Young Jung),이기현(Gi Hyun Lee),장정우(Jeong Woo Jang),윤진미(Jinmi Yoon),라비굽타(Ravi Gupta),김선태(Sun Tae Kim),민철우(Cheol Woo Min) 한국식물생명공학회 2021 JOURNAL OF PLANT BIOTECHNOLOGY Vol.48 No.3
The solubilization of isolated proteins into the adequate buffer containing of surfactants is primary step for proteomic analysis. Particularly, sodium dodecyl sulfate (SDS) is the most widely used surfactant, however, it is not compatible with mass spectrometry (MS). Therefore, it must be removed prior to MS analysis through rigorous washing, which eventually results in inevitable loss. Recently, photocleavable surfactant, 4-hexylphenylazosulfonate (Azo), was reported which can be easily degraded by UV irradiation and is compatible with MS during proteomic approach using animal tissues. In this study, we employed comparative label-free proteomic analysis for evaluating the solubilization efficacy of the Azo and SDS surfactants using rice leave samples. This approach led to identification of 3,365 proteins and out of 682 proteins were determined as significantly modulated. Further, according to the subcellular localization prediction in SDS and Azo, proteins localized in the chloroplast were the major organelle accounting for 64% of the total organelle in the SDS sample, while only 37.5% of organelle proteins solubilized in the Azo were predicted to be localized in chloroplast. Taken together, this study validates the efficient solubilization of total protein isolated from plant material for bottom-up proteomics. Azo surfactant is suitable as substituents of SDS and promising for bottomup proteomics as it facilitates robust protein extraction, rapid washing step during enzymatic digestion, and MS analysis.