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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
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dc.contributor.advisor | 金洛仁(Laurent Zimmerli) | |
dc.contributor.author | Hsien-Wei Mai | en |
dc.contributor.author | 麥賢偉 | zh_TW |
dc.date.accessioned | 2021-07-11T14:45:19Z | - |
dc.date.available | 2021-08-02 | |
dc.date.copyright | 2016-08-02 | |
dc.date.issued | 2016 | |
dc.date.submitted | 2016-07-28 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/78190 | - |
dc.description.abstract | 在阿拉伯芥植物中有許多L型態凝集素受體激酶(LecRKs)參與病原菌辨識機制中引起細胞內對抗生物性跟非生物性的逆境防禦機制。此種受體激酶有細胞外的豆科植物凝集素區域,穿膜區域和細胞內的絲氨酸/蘇氨酸激酶區域。在我們實驗室先前研究發現LecRK-V.2和LecRK-VII.1都參與在病原菌防禦機制當中。此兩基因突變株比起野生型Col-0阿拉伯芥對抗Pseudomonas syringae pv. tomato DC3000 (Pst DC3000)此病的能力來得弱;然而,此兩基因過量表現轉殖株則相較野生型對抗Pst DC3000的抗性更強,並且我們發現此兩基因突變株在氣孔的免疫機制上有明顯的缺陷。在此,我們利用阿拉伯芥原生質體過量表現此兩基因蛋白質再利用共免疫沉澱法去偵測兩蛋白質對於鞭毛蛋白辨識受體FLS2和其複合體蛋白質BAK1是否有與此免疫複合體產生結合的情形。我們也在酵母菌雙雜合系統實驗發現LecRK-V.2 和LecRK-VII.1蛋白質可以透過內部激酶區域與FLS2及BAK1蛋白質內部激酶區域產生結合的現象。為了更加瞭解此兩基因參與的植物抗病菌的防禦機制調控,在此研究,我們發現此兩基因參與在細菌鞭毛蛋白引起植物體免疫防禦機制的FLS2-BAK1複合體當中。 | zh_TW |
dc.description.abstract | In Arabidopsis, several L-type lectin receptor kinases (LecRKs) were found to function as or together with pattern-recognition receptors (PRRs) in recognition of stress signals and initiation of plant defense responses towards abiotic and biotic stresses. LecRKs possess an extracellular legume-lectin domain, a transmembrane domain and an intracellular serine/threonine kinase domain. Our previous analyses show that LecRK-V.2 and LecRK-VII.1 are involved in the pattern-triggered immunity (PTI) defense response. Both lecrk-V.2 and lecrk-VII.1 mutant plants are indeed more susceptible to bacteria Pseudomonas syringae pv. tomato DC3000 than Col-0 wild-type plants. LecRK-V.2 and LecRK-VII.1 overexpression lines demonstrate increased resistance to Pst DC3000. In addition, both lecrk-V.2 and lecrk-VII.1 mutants are defective in stomatal immunity. Here, we show by co-immunoprecipitation in Arabidopsis protoplast that LecRK-V.2 and LecRK-VII.1 associated with the PRR FLS2 and the co-receptor BAK1 before and after perception of the bacterial pathogen-associated molecular pattern (PAMP) flagellin. Moreover, LecRK-V.2 and LecRK-VII.1 could interact with FLS2 and BAK1 through their kinase domains when analyzed by the in vitro yeast-two-hybrid assay. In this study, I clarified the role of LecRK-V.2 and LecRK-VII.1 in the FLS2-BAK1 complex upon flagellin perception. | en |
dc.description.provenance | Made available in DSpace on 2021-07-11T14:45:19Z (GMT). No. of bitstreams: 1 ntu-105-R03b42007-1.pdf: 1826027 bytes, checksum: 7dc6d80549dc11e51dd3d853457effc4 (MD5) Previous issue date: 2016 | en |
dc.description.tableofcontents | 摘要 II
Abstract IV Contents VI Introduction 1 Material and Methods 9 Biological Material and Plant Growth Conditions 9 Co-immunoprecipitation Assay in Arabidopsis Protoplast. 9 Yeast Two-Hybrid Assays 11 Results 14 LecRK-V.2 and LecRK-VII.1 associate with FLS2 in vivo 14 LecRK-VII.1 could directly interact with FLS2 through their kinase domain, but LecRK-V.2 could not. 15 LecRK-V.2 and LecRK-VII.1 associate with BAK1 in vivo 16 In vitro, BAK1 can directly interact with LecRK-V.2 and LecRK-VII.1 through their kinase domain 17 In vitro and in vivo association analyses of LecRK-V.2 and LecRK-VII.1 18 Each LecRKs may not affect the association of FLS2 with the other LecRK 20 Discussion 22 Conclusions and Future Perspectives 27 Figures 30 Figure 1:FLS2 associate with LecRK-V.2 and LecRK-VII.1 when analyzed by co-immunoprecipitation in Arabidopsis protoplasts. 30 Figure 2:In vitro FLS2 direct interaction with LecRK-VII.1 kinase domains but not LecRK-V.2. 32 Figure 3:BAK1 associates with LecRK-V.2 and LecRK-VII.1 when analyzed by co-immunoprecipitation in Arabidopsis protoplasts. 33 Figure 4:BAK1 can directly interact with LecRK-V.2 and LecRK-VII.1 through its kinase domain. 35 Figure 5: Co-immunoprecipitation analyses of LecRK-V.2 association with LecRK-VII.1 in Arabidopsis protoplasts. 36 Figure 6: LecRK-V.2 cannot directly interact with LecRK-VII.1 through their kinase domain when analyzed with the yeast two hybrid assay. 38 Figure 7: FLS2 associates with BAK1 and LecRK-VII.1 in the lecrk-V.2 mutant background. 39 Figure 8: FLS2 associates with BAK1 and LecRK-V.2 in the lecrk-VII.1 mutant background. 40 Figure 9:Proposed model 41 Tables 43 Table 1 :Primers for kinase domain constructs 43 Table 2 :List of abbreviations 44 Supplementary Figures 45 Supplemental Figure 1: LecRK-V.2 and LecRK-VII.1 are necessary for the resistance against to Pst.DC3000. 45 Supplemental Figure 2: LecRK-V.2 and LecRK-VII.1 are necessary for stomatal immunity. 46 Supplemental Figure 3:The PTI apoplastic responses and regulations in lecrk-V.2 and lecrk-VII.1 mutant lines. 47 Supplemental Figure 4:LecRK-V.2-GFP and LecRK-VII.1 –GFP fusion proteins localized on the membrane in Arabidopsis mesophyll protoplast. 49 References 52 | |
dc.language.iso | en | |
dc.title | 阿拉伯芥中LecRK-V.2和LecRK-VII.1蛋白質在處理細菌鞭毛蛋白後與辨識鞭毛蛋白受體FLS2和其共同受體BAK1的蛋白質複合體形成之分析 | zh_TW |
dc.title | Analysis of LecRK-V.2 and LecRK-VII.1 complex
formation with FLS2 and BAK1 upon flagellin perception in Arabidopsis | en |
dc.type | Thesis | |
dc.date.schoolyear | 104-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 吳克強(Keqiang Wu),鄭貽生(Yi-Sheng Cheng),王雅筠(Ya-Yun Wang) | |
dc.subject.keyword | 阿拉伯芥,LecRK-V.2,LecRK-VII.1,病原菌辨識受體,防禦機制,FLS2,BAK1, | zh_TW |
dc.subject.keyword | FLS2,LecRK-V.2,LecRK-VII.1,BAK1,stomatal closure,Pst DC3000,PTI, | en |
dc.relation.page | 56 | |
dc.identifier.doi | 10.6342/NTU201601482 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2016-07-28 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 植物科學研究所 | zh_TW |
顯示於系所單位: | 植物科學研究所 |
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