Abstract Detail

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