Functional Mode of NtHSP17.6, a Cytosolic Small Heat-Shock Protein from Nicotiana tabacum
- Authors
- Yoon, Hae-jung; Kim, Keun Pil; Park, Soo Min; Hong, Choo Bong
- Issue Date
- Mar-2005
- Publisher
- 한국식물학회
- Keywords
- in vitro activity; Luciferase; Luc; molecular chaperone; small heat-shock protein; sHsp
- Citation
- Journal of Plant Biology, v.48, no.1, pp 120 - 127
- Pages
- 8
- Journal Title
- Journal of Plant Biology
- Volume
- 48
- Number
- 1
- Start Page
- 120
- End Page
- 127
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/58923
- DOI
- 10.1007/BF03030571
- ISSN
- 1226-9239
1867-0725
- Abstract
- Small heat-shock proteins (sHsps) are ubiquitous stress proteins with molecular chaperone activity. They share characteristic homology with the α-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, NtHSP17.6, from Nicotiana tabacum, and analyzed its functional mode for such activity. Following its transformation into Escherichia colt and its over-expression, NtHSP17.6 was purified and examined in vitro. This purified NtHSP17.6 exhibited typical chaperone activity in a light-scattering test. It was enable to protect a model substrate, firefly luciferase, from heat-induced aggregation. Non-denaturing 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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