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

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28 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 languageEnglish
Pages (from-to)1341-1348
Number of pages8
JournalPlant and Cell Physiology
Volume36
Issue number7
StatePublished - Oct 1995

Keywords

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

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