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논문 기본 정보

자료유형
학술저널
저자정보
Yoon Hae-jeong (Institute of Molecular Biology and Genetics, Seoul National University) Kim Keun Pill (Institute of Molecular Biology and Genetics, Seoul National University) Park Soo Min (Institute of Molecular Biology and Genetics, Seoul National University) Hong Choo Bong (Institute of Molecular Biology and Genetics, Seoul National University)
저널정보
한국식물학회 식물학회지 식물학회지 제48권 제1호
발행연도
2005.1
수록면
120 - 127 (8page)

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Small heat-shock proteins (sHsps) are ubiquitous stress proteins with molecular chaperone activity. They share characteristic homology with the $\alpha-crystallin$ protein of the mammalian eye lens as well as being ATP. independent in their chaperone activity. We isolated a clone for a cytosolic class I sHsp, NtHSPI7.6, from Nicotiana tabacum, and analyzed its functional mode for such activity. Following its transformation into Escherichia coli and its over-expression, NtHSP17.6 was purified and examined in vitro. This purified NtHSP17.6 exhibited typical chaperone activity in a light­scattering test It was enable to protect a model substrate, firefly luciferase, from heat-induced aggregation. Non­denaturing PAGE showed that NtHSP17.6 formed a dodecamer in its native conformation, and was bound to its substrate under heat stress. A labeling test with bis-ANS indicated that this binding might be linked to newly exposed hydrophobic sites of the NtHSP17.6 complexes during heat shock. Based on these data, we suggest that NtHSP17.6 is a molecular chaperone that functions as a dodecamer in a heat-induced manner.

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