DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Park, Chankyu | - |
dc.contributor.advisor | 박찬규 | - |
dc.contributor.author | Kim, Jihong | - |
dc.contributor.author | 김지홍 | - |
dc.date.accessioned | 2018-05-23T19:34:34Z | - |
dc.date.available | 2018-05-23T19:34:34Z | - |
dc.date.issued | 2017 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=675720&flag=dissertation | en_US |
dc.identifier.uri | http://hdl.handle.net/10203/241839 | - |
dc.description | 학위논문(박사) - 한국과학기술원 : 생명과학과, 2017.2,[iii, 55 p. :] | - |
dc.description.abstract | Hsp31 protein belongs to the DJ-1/ThiJ/PfpI superfamily, and increases the survival of Escherichia coli in stressful conditions. It was initially reported as a holding chaperone, and its glyoxalase III activity has recently been characterized. Although Hsp31 becomes a high molecular weight form at $60 ^\circ C$ ($HMW_{Heat}$) that has an enhanced chaperone activity compared to the native dimer, the HMWHeat doesn’t seem to have a biological relevance due to the high temperature. Here, we reported a novel mechanism by which the $Zn^{+2}$ -mediated high molecular weight form ($HMW_{Znic}$) of Hsp31 occurred at $50 ^\circ C$ and acquired an increased chaperone activity. Moreover, the $HMW_{Znic}$ was reversible to the native dimer by EDTA-incubation. The analyses of the chromatographic intermediate between the native dimer and the HMWZnic, which was stabilized by the $Ni^{+2}$ incorporation, revealed that the unfolding of the N-terminal long loop and the C-terminal $\alpha$ -helix led to the exposure of the hydrophobic interior. The $H_2O_2$ -treatment accelerated the $HM_{Znic}$ formation of Hsp31, and the C185E mutant mimicking the Cys oxidation was able to form the $HMW_{Znic}$ even at $45 ^\circ C$. Two distinct characteristics of the $HMW_{Znic}$ formation (the reversibility and the need for a low $Zn^{+2}$ concentration) shed a clue on the regulatory mechanism of Hsp31 via the structural change for the glyoxalase III and chaperone activities. | - |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | Hsp31 | - |
dc.subject | high molecular weight | - |
dc.subject | chaperone | - |
dc.subject | zinc | - |
dc.subject | oligomerization | - |
dc.subject | 고분자형태 | - |
dc.subject | 샤페론 | - |
dc.subject | 아연 | - |
dc.subject | 올리고머화 | - |
dc.title | Regulation of Hsp31 chaperone activity by metal-induced structural change | - |
dc.title.alternative | 금속으로 유도되는 구조적 변화에 의한 Hsp31 샤페론 활성의 조절 | - |
dc.type | Thesis(Ph.D) | - |
dc.identifier.CNRN | 325007 | - |
dc.description.department | 한국과학기술원 :생명과학과, | - |
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