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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/17223
Title: | 阿拉伯芥粒線體GrpE蛋白質之熱穩定性研究 Thermostability Analysis of Two Arabidopsis Mitochondrial GrpE Proteins |
Authors: | Zih-teng Chen 陳子騰 |
Advisor: | 常怡雍(Yee-yung Charng) |
Co-Advisor: | 楊健志(Chien-chih Yang) |
Keyword: | 阿拉伯芥,GrpE,Mge,熱穩定性, Arabidopsis,GrpE,Mge,thermostability, |
Publication Year : | 2013 |
Degree: | 碩士 |
Abstract: | Prokaryotic GrpE acts as a nucleotide-exchange factor in the Hsp70/DnaK chaperone machinery. Two GrpE homologs were identified in Arabidopsis mitochondria (Mge1 and Mge2). Mge2, but not Mge1, restores the growth of heat-sensitive E. coli grpE mutant, DA16, at 43 oC. Although Mge1 and Mge2 are highly similar in primary structure, Mge2 possesses an extra peptide derived from a retained in-frame intron sequence. Phenotyping of Mge2 T-DNA knockout lines reveals that Mge2 is specifically required for tolerating prolonged exposure to moderately high temperature. To characterize how Mge2 confers tolerance to high temperature, plasmids expressing recombinant Mge proteins were constructed and used for complementary assay. Recombinant Mge proteins were purified and analyzed by circular dichroism. The results suggested Mge2 was more thermostable than Mge1. And the in-frame intron-derived peptide sequence of Mge2 might not affect the thermostability in vitro. Furthermore, analysis of domain-swapped Mge proteins indicated that both the long α-helix domain and the β-sheet domain might affect the thermostability of Mge proteins, but the long α-helix domain might be predominant in affecting the thermostability. |
URI: | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/17223 |
Fulltext Rights: | 未授權 |
Appears in Collections: | 生化科技學系 |
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ntu-102-1.pdf Restricted Access | 2.69 MB | Adobe PDF |
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