Functional Mode of NtHSP17.6, a Cytosolic Small Heat-Shock Protein from Nicotiana tabacum

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 sHs...

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Bibliographic Details
Published in:Journal of plant biology = Singmul Hakhoe chi 2005-03, Vol.48 (1)
Main Authors: 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
Format: Article
Language:English
Subjects:
in vitro activity
luciferase (Luc)
molecular chaperone
NICOTIANA TABACUM
small heat-shock protein (sHsp)
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Summary: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.
ISSN:1226-9239
1867-0725
DOI:10.1007/BF03030571