Abstract
A study was conducted on the molecular mechanism of small heat shock proteins (sHSPs) in Chaetomium globosum. Heat shock protein 22.4 (Hsp22.4) from C. globosum was cloned and expressed in Escherichia coli. BlastX analysis revealed that the Hsp22.4 gene from C. globosum shared the highest identity in amino acid sequence with a Hsp gene from Neurospora crassa, and the identity between them was 65%. The C. globosum Hsp22.4 gene was inserted into the expressive vector of pGEX-4T-2 and the recombinant plasmid named pGEX-HSP. E. coli BL21 transformed with pGEX-HSP plasmid was induced by IPTG, and the expressed proteins were analyzed with SDS-PAGE. A 50 kD protein was specially expressed in E. coli BL21, and the result was consistent with expectation, and showed that the Hsp22.4 gene had been expressed in E. coli. Our study has made a foundation for further studying the function of sHSPs protein.
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Biography: LIU Zhi-hua (1976–), female, Ph.D., Department of Life Science and Engineering, Harb in Institute of Technology, Harbin 150001, P. R. China
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Liu, Zh., Yang, Q. & Nie, Yh. Cloning and expression of Hsp22.4 gene from Chaetomium globosum . J. of For. Res. 17, 259–262 (2006). https://doi.org/10.1007/s11676-006-0059-4
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DOI: https://doi.org/10.1007/s11676-006-0059-4