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Physiological Section

Sung, Wei-wen [1], Chen, Yung-reui [1], Lin, Chu-yung [1].

Immunolocalization and Thermostablity of a Rice 16.9 kDa Heat Shock Protein Expressed in Escherichia. coli.

A gene encoding the rice 16.9-kDa class I low-molecular-mass (LMM) heat-shock protein (HSP), Oshsp16.9, was introduced into Escherichia coli using the pUC8 expression vector. Its expression affecting on thermotolerance and its localization in microbes were studied under heat shock. When E. coli cells transformed with recombinant plasmid, pUC-FL cells (containing Oshsp16.9 cDNA and pUC8) were under the pretreatment of isopropyl-D-thiogalactopyranoside (IPTG) for 6 h, the survivability of the pUC-FL cells after heat-shocked at 50° for 1 h was 40 fold higher than that of control cells (transformed with pUC8 only). Ultrastructural studies demonstrated that after transferring to 37°, the heat shocked pUC-FL cells could be recovery from heat damage, such as partial plasmolysis and protein aggregation. Immunogoldal localization showed that IPTG induction of HSP performed distinctly in pUC-FL cells and the gold particles mainly distributed in cytoplasm of E. coli. Quantitative comparison of gold particles in cells under different treatment demonstrated that there was a distinct difference in Oshsp16.9 expressed cells with or without IPTG pretreated.


1 - National Taiwan University, Taipei, 106, Taiwan

Keywords:
Escherichia coli
immunolocalization
rice hsp gene
thermotolerance.

Presentation Type: Paper
Session: 11-1
Location: White Pine (Cliff Lodge)
Date: Monday, August 2nd, 2004
Time: 10:00 AM
Abstract ID:33


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