A recombinant rice 16.9-kda heat shock protein can provide thermoprotection in vitro

Ching Hui Yeh; Kai Wun Yeh; Shu Hsing Wu; Pi Fang Linda Chang; Yih Ming Chen; Chu Yung Lin

A recombinant rice 16.9-kda heat shock protein can provide thermoprotection in vitro

Ching Hui Yeh, Kai Wun Yeh, Shu Hsing Wu, Pi Fang Linda Chang, Yih Ming Chen, Chu Yung Lin

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

It is difficult to obtain large amounts of purified low-molecular-mass heat shock proteins (LMM HSPs), which are unique to plants, for biochemical and physiological studies. Therefore, an attempt was made to produce such a HSP by applying recombinant DNA technology. We fused the cDNA for a rice class I 16.9-kDa HSP, pTSl, to the gene for glutathione S-transferase (GST) of Schistosoma japonicum and we obtained large amounts of the fusion protein from transformed Escherichia coli cells. In addition, we found that the 16.9-kDa HSP obtained by cleavage of the recombinant protein could also form a protein complex of ̃310 kDa under non-denaturing conditions as can the small, native, class I HSPs from heat-shocked rice seedlings. An assay in vitro to examine the thermoprotection of rice soluble proteins from heat denaturation revealed the strong stabilizing effect of the recombinant HSP.

Original language	English
Pages (from-to)	1341-1348
Number of pages	8
Journal	Plant and Cell Physiology
Volume	36
Issue number	7
State	Published - Oct 1995

Keywords

Expression in E. coli
Low-molecular-mass heat shock proteins
Rice
Thermoprotection

Cite this

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title = "A recombinant rice 16.9-kda heat shock protein can provide thermoprotection in vitro",

abstract = "It is difficult to obtain large amounts of purified low-molecular-mass heat shock proteins (LMM HSPs), which are unique to plants, for biochemical and physiological studies. Therefore, an attempt was made to produce such a HSP by applying recombinant DNA technology. We fused the cDNA for a rice class I 16.9-kDa HSP, pTSl, to the gene for glutathione S-transferase (GST) of Schistosoma japonicum and we obtained large amounts of the fusion protein from transformed Escherichia coli cells. In addition, we found that the 16.9-kDa HSP obtained by cleavage of the recombinant protein could also form a protein complex of{\~ }310 kDa under non-denaturing conditions as can the small, native, class I HSPs from heat-shocked rice seedlings. An assay in vitro to examine the thermoprotection of rice soluble proteins from heat denaturation revealed the strong stabilizing effect of the recombinant HSP.",

keywords = "Expression in E. coli, Low-molecular-mass heat shock proteins, Rice, Thermoprotection",

author = "Yeh, {Ching Hui} and Yeh, {Kai Wun} and Wu, {Shu Hsing} and Chang, {Pi Fang Linda} and Chen, {Yih Ming} and Lin, {Chu Yung}",

note = "Funding Information: Supported by grants (NSC81-0211-B0O2-13 and NSC82-0211-B002-241) to C.Y. Lin from the National Science Council of Taiwan. 1 To whom correspondence should be addressed.",

year = "1995",

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volume = "36",

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TY - JOUR

T1 - A recombinant rice 16.9-kda heat shock protein can provide thermoprotection in vitro

AU - Yeh, Ching Hui

AU - Yeh, Kai Wun

AU - Wu, Shu Hsing

AU - Chang, Pi Fang Linda

AU - Chen, Yih Ming

AU - Lin, Chu Yung

N1 - Funding Information: Supported by grants (NSC81-0211-B0O2-13 and NSC82-0211-B002-241) to C.Y. Lin from the National Science Council of Taiwan. 1 To whom correspondence should be addressed.

PY - 1995/10

Y1 - 1995/10

N2 - It is difficult to obtain large amounts of purified low-molecular-mass heat shock proteins (LMM HSPs), which are unique to plants, for biochemical and physiological studies. Therefore, an attempt was made to produce such a HSP by applying recombinant DNA technology. We fused the cDNA for a rice class I 16.9-kDa HSP, pTSl, to the gene for glutathione S-transferase (GST) of Schistosoma japonicum and we obtained large amounts of the fusion protein from transformed Escherichia coli cells. In addition, we found that the 16.9-kDa HSP obtained by cleavage of the recombinant protein could also form a protein complex of ̃310 kDa under non-denaturing conditions as can the small, native, class I HSPs from heat-shocked rice seedlings. An assay in vitro to examine the thermoprotection of rice soluble proteins from heat denaturation revealed the strong stabilizing effect of the recombinant HSP.

AB - It is difficult to obtain large amounts of purified low-molecular-mass heat shock proteins (LMM HSPs), which are unique to plants, for biochemical and physiological studies. Therefore, an attempt was made to produce such a HSP by applying recombinant DNA technology. We fused the cDNA for a rice class I 16.9-kDa HSP, pTSl, to the gene for glutathione S-transferase (GST) of Schistosoma japonicum and we obtained large amounts of the fusion protein from transformed Escherichia coli cells. In addition, we found that the 16.9-kDa HSP obtained by cleavage of the recombinant protein could also form a protein complex of ̃310 kDa under non-denaturing conditions as can the small, native, class I HSPs from heat-shocked rice seedlings. An assay in vitro to examine the thermoprotection of rice soluble proteins from heat denaturation revealed the strong stabilizing effect of the recombinant HSP.

KW - Expression in E. coli

KW - Low-molecular-mass heat shock proteins

KW - Rice

KW - Thermoprotection

UR - http://www.scopus.com/inward/record.url?scp=0029392520&partnerID=8YFLogxK

M3 - 期刊論文

C2 - 8564303

AN - SCOPUS:0029392520

SN - 0032-0781

VL - 36

SP - 1341

EP - 1348

JO - Plant and Cell Physiology

JF - Plant and Cell Physiology

IS - 7

ER -

A recombinant rice 16.9-kda heat shock protein can provide thermoprotection in vitro

Abstract

Keywords

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