Functional Mode of NtHSP17.6, a Cytosolic Small Heat-Shock Protein from Nicotiana tabacum
2005
Yoon, H.J. (Seoul National University, Seoul, Republic of Korea) | Kim, K.P. (Seoul National University, Seoul, Republic of Korea) | Park, S.M. (Seoul National University, Seoul, Republic of Korea) | Hong, C.B. (Seoul National University, Seoul, Republic of Korea), E-mail: hcb@snu.ac.kr
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 coli and its over-expression, NtHSP17.6 was purified and examined in vitro.
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