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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 | Fu-Chun Liang | en |
dc.contributor.author | 梁富淳 | zh_TW |
dc.date.accessioned | 2021-07-11T14:40:55Z | - |
dc.date.available | 2022-02-20 | |
dc.date.copyright | 2017-02-20 | |
dc.date.issued | 2016 | |
dc.date.submitted | 2016-09-29 | |
dc.identifier.citation | Acharya, B. R., and Assmann, S. M. (2009). Hormone interactions in stomatal function. Plant Mol. Biol. 69: 451–462.
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/78057 | - |
dc.description.abstract | 植物會藉由細胞膜上的模式辨識受體 (PRR) 來辨識病原菌相關分子模式 (PAMPs) ,並啟動下游的防禦反應。透過分析微陣列資訊及T-DNA 插入型突變的表型,Zimmerli實驗室選了L型凝集素類受體激酶V.2 (LecRK-V.2) 及VII.1 (LecRK-VII.1) 做更深入的研究。LecRK包含了胞外的豆科植物凝集素結構域、穿膜結構域以及胞內的激酶結構域。這兩個基因剔除突變種對於由細菌、PAMP或茉莉酸所引起的氣孔關閉皆不敏感。在此篇碩士論文中,透過重複lecrk-V.2及lecrk-VII.1的感染及氣孔實驗,我證實了先前的研究結果。由於只有一個lecrk-V.2的突變株,我將由原生啟動子所引導的LecRK-V.2表現在lecrk-V.2突變株中,用以確認在lecrk-V.2突變株種中受損的防禦反應是咎因於LecRK-V.2的失能。透過磷酸化染劑發現LecRK蛋白是有活性的激酶,其中,轉殖了失去激酶活性LecRK的lecrk回復株對於細菌和PAMP的反應是一樣的,表示這些失去激酶活性的LecRK無法補償突變種中受損的氣孔反應。雙分子螢光互補法顯示這兩個LecRK分別只會在處理PAMP之後與PRR─FLS2進行交互作用,反之,不論有否PAMP處理,LecRK都會跟FLS2的共同受體BAK1交互作用。此外,在互相的lecrk突變種中,LecRK都不能跟FLS2進行交互作用,而失去激酶活性的LecRK則可以在沒有PAMP處理之下就跟FLS2接觸。總體而言,這些實驗結果指出,LecRK-V.2和LecRK-VII.1都參與在阿拉伯芥氣孔的免疫系統中,而且他們的激酶活性對功能非常重要。 | zh_TW |
dc.description.abstract | Plants recognize pathogen/microbe-associated molecular patterns (PAMPs/MAMPs) by cell-membrane localized pattern recognition receptors (PRRs) to activate downstream PAMP-triggered immunity (PTI) responses. Analyzing microarray profiles and T-DNA insertion mutant phenotypes, the Zimmerli laboratory selected two legume-like lectin receptor kinases (LecRKs), LecRK-V.2 and LecRK-VII.1 for further characterization. LecRKs possess an extracellular legume-like lectin domain, a transmembrane domain and an intracellular kinase domain. Both lecrk-V.2 and lecrk-VII.1 knock-out mutants were insensitive to bacteria-, PAMP- and MeJA-induced stomatal closure. In this master thesis, I confirmed preliminary data by repeating infection and stomatal aperture assays in lecrk-V.2 and lecrk-VII.1 mutants. Since only one T-DNA insertion knock-out mutant could be isolated for LecRK-V.2, lecrk-V.2-1 / NP: LecRK-V.2-GFP lines were generated to confirm that impaired defense responses in the lecrk-V.2 mutant were caused by loss-of-function of LecRK-V.2. In addition, phosphorylation analyses revealed that both LecRKs are active kinases. Notably, stomata of lecrk mutants transformed with LecRK dead kinase version, lecrk-V.2-1 / 35S: LecRK-V.2D459A-GFP and lecrk-VII.1-1 / 35S: LecRK-VII.1D475A-GFP responded to bacteria and PAMPs as mutant lines, suggesting that these constructs could not complement the defective stomatal closure of lecrk mutants. Furthermore, interaction analyses with the bimolecular fluorescence complementation technique suggested that LecRK-V.2 and LecRK-VII.1 only directly interacted with the PRR FLS2 after treatment with the PAMP flg22. By contrast, both LecRKs interacted with the FLS2 co-receptor BAK1 independently of flg22 treatment. In addition, LecRK-V.2 and LecRK-VII.1 failed to interact with FLS2 in the other mutant background and dead kinase version of both LecRKs directly interacted with FLS2, even before flg22 treatment. Taken together, these data suggest that LecRK-V.2 and LecRK-VII.1 are both involved in stomatal immunity at the PRR FLS2 complex, and their kinase activities are critical for their functions. | en |
dc.description.provenance | Made available in DSpace on 2021-07-11T14:40:55Z (GMT). No. of bitstreams: 1 ntu-105-R03b42010-1.pdf: 3392391 bytes, checksum: 451d730367334ed47ec4cc64906df0d7 (MD5) Previous issue date: 2016 | en |
dc.description.tableofcontents | 誌謝 II
摘要 III Abstract IV Content VI Introduction 1 Pathogen/microbe-associated molecular patterns (PAMPs/MAMPs) and pattern recognition receptors (PRRs) 1 PAMP-triggered Immunity (PTI) 2 Salicylic acid and jasmonate - ethylene defense responses 2 Stomatal immunity 3 Lectin receptor kinases 4 Materials and methods 7 Plant growth conditions 7 Generation of transgenic lines 7 Plant transformation 8 Disease assay 9 Stomatal aperture assay 10 Recombinant protein expression 10 Pro-Q Diamond assay 12 Bimolecular fluorescence complementation (BiFC) 13 Accession numbers 13 Results 14 LecRK-V.2 and LecRK-VII.1 are necessary for resistance toward hemi-biotrophic bacteria 14 Stomata of lecrk-V.2 and lecrk-VII.1 are less sensitive to PAMP-induced stomatal closure 14 Stomata of lecrk-V.2 and lecrk-VII.1 are insensitive to MeJA-induced stomatal closure 15 LecRK-V.2 complementation lines restore stomatal aperture to the wild type level 16 LecRK-V.2 and LecRK-VII.1 interact with FLS2 and BAK1 17 Both LecRKs fail to interact with FLS2 after flg22 treatment in the other lecrk mutant background 18 LecRK-V.2D459A and LecRK-VII.1D475A possess a defective kinase activity 19 LecRK-V.2D459A and LecRK-VII.1D475A fail to complement lecrk-V.2 and lecrk-VII.1 phenotypes 20 LecRK-V.2D459A and LecRK-VII.1D475A interact with FLS2 before and after PAMP treatment 21 Discussion 22 The non-redundancy of LecRK-V.2 and LecRK-VII.1 22 The insensitivities of LecRK-V.2 and LecRK-VII.1 toward MeJA 22 The interaction of the FLS2 complex with LecRK-V.2 and LecRK-VII.1 23 The band-shift of LecRK-V.2-GST after auto-phosphorylation 24 Conclusion and future perspectives 26 Figures 28 Figure 1. Disease responses of lecrk-V.2 and lecrk-VII.1 mutants against Pst DC3000. 28 Figure 2. Stomatal immunity in lecrk-V.2 and lecrk-VII.1 mutants. 30 Figure 3. Stomatal responses of lecrk-V.2 and lecrk-VII.1 mutants toward MeJA. 33 Figure 4. Stomatal immunity of LecRKV.2 complementation lines. 35 Figure 5. Stomatal responses of LecRKV.2 complementation lines toward hormones. 37 Figure 6. Interaction of FLS2 and BAK1 with LecRK-V.2 and LecRK-VII.1 in Col-0 protoplasts. 38 Figure 7. Interaction between FLS2 and LecRK-V.2 or LecRK-VII.1 in the other lecrk mutant protoplast. 40 Figure 8. Phosphorylation status of LecRK-V.2 and LecRK-VII.1. 41 Figure 9. Stomatal immunity of dead kinase version of LecRK-V.2D459A and LecRK-VII.1D475A complementation lines. 45 Figure 10. Stomatal responses of dead kinase version LecRK-V.2D459A and LecRK-VII.1D475A complementation lines toward hormones. 47 Figure 11. Interaction between FLS2 and the dead kinase versions of LecRK-V.2D459A or LecRK-VII.1D475A in Col-0 protoplast. 49 Supplementary Figures 50 Figure S1. T-DNA insertion lines of LecRK-V.2 and LecRK-VII.1. 50 Figure S2. Cellular localization of LecRK-V.2 and LecRK-VII.1. 51 Figure S3. Apoplastic PTI of lecrk-V.2 and lecrk-VII.1 mutants. 53 Figure S4. Stomatal responses of lecrk-V.2 and lecrk-VII.1 mutants toward hormones. 54 Figure S5. In vivo association between FLS2 and BAK1 with LecRK-V.2 or LecRK-VII.1. 55 Table 56 Table 1. Primer sequences used for constructs 56 Supplementary Table 57 Table S1. The lecrk mutants selected for Pst DC3000 infection 57 Appendix 58 Appendix I. Media used for Arabidopsis seedling culture 58 Appendix II. Media used for bacteria culture 58 Appendix III. The buffers used in Pro-Q Diamond assay 59 References 60 | |
dc.language.iso | en | |
dc.title | LecRK-V.2及LecRK-VII.1在阿拉伯芥氣孔防禦反應中的功能性分析 | zh_TW |
dc.title | Functional analysis of LecRK-V.2 and LecRK-VII.1 in Arabidopsis thaliana stomatal immunity | en |
dc.type | Thesis | |
dc.date.schoolyear | 105-1 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 林讚標,吳克強,張英?,林乃君 | |
dc.subject.keyword | 阿拉伯芥,LecRK,防禦反應,氣孔免疫系統,茉莉酸,激?活性, | zh_TW |
dc.subject.keyword | Arabidopsis,legume-like lectin receptor kinase,PAMP-triggered immunity,stomatal immunity,jasmonate,kinase activity, | en |
dc.relation.page | 64 | |
dc.identifier.doi | 10.6342/NTU201603627 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2016-09-29 | |
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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