Tobacco small heat-shock protein, NtHSP18.2, has broad substrate range as a molecular chaperone

Small heat-shock proteins have been strongly implicated in heat tolerance in plants. We isolated a full-length cDNA clone, NtHSP18.2, from tobacco that encoded a cytosolic class I small heat-shock protein. For in vitro functional analysis of NtHSP18.2, it has been overproduced in Escherichia coli an...

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Bibliographic Details
Published in:Plant science (Limerick) 2004-11, Vol.167 (5), p.1017-1025
Main Authors: Kim, Keun Pill, Joe, Myung Kook, Hong, Choo Bong
Format: Article
Language:English
Subjects:
Atomic force microscopy
Biological and medical sciences
citrate (si)-synthase
complementary DNA
Escherichia coli
Fundamental and applied biological sciences. Psychology
gene expression
Genes. Genome
glyceraldehyde-3-phosphate dehydrogenase
heat shock proteins
Molecular and cellular biology
Molecular chaperone
molecular chaperones
Molecular genetics
Nicotiana tabacum
NtHSP18.2
plant proteins
protein aggregates
purification
Small heat-shock protein
tobacco
Two-dimensional gel
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Summary:Small heat-shock proteins have been strongly implicated in heat tolerance in plants. We isolated a full-length cDNA clone, NtHSP18.2, from tobacco that encoded a cytosolic class I small heat-shock protein. For in vitro functional analysis of NtHSP18.2, it has been overproduced in Escherichia coli and purified. Measurement of light scattering at 320 nm for citrate synthase (CS) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), heat labile proteins, after heat treatment indicated that NtHSP18.2 prevents aggregation of non-native CS and GAPDH during heat-shock treatment. The complexes of NtHSP18.2 and CS were visualized by atomic force microscopy. The image revealed that the complex is in granule form, and the granules were NtHSP18.2 based. When E. coli cellular proteins were subjected to the molecular chaperone activity of NtHSP18.2, a large portion of the E. coli cellular proteins were forming complexes with NtHSP18.2 and remained soluble. This broad substrate range of NtHSP18.2 molecular chaperone activity could be shown by two-dimensional gel analysis as well.
ISSN:0168-9452
1873-2259
DOI:10.1016/j.plantsci.2004.05.043