Cloning and expression of Hsp22.4 gene from Chaetomium globosum

研究在 Chaetomium globosum 在小热吃惊蛋白质(sHSPs ) 的分子的机制上被进行。热吃惊蛋白质 22.4 (Hsp22.4 ) 从 C。globosum 在 Escherichia 关口 i 被克隆并且表示。BlastX 分析揭示了从 C 的 Hsp22.4 基因。globosumshared 在有从 Neurospora 的 Hsp 基因的氨基酸顺序的最高的身份粗糙一，并且在他们之间的身份是 65% 。C。globosum Hsp22.4 基因被插入到 pGEX-4T-2 的富有表达力的向量，重组体原生质标志说出 pGEX-HSP。E。与 pGEX-HSPplasmid 转变的关口 i BL21 被 IPTG 导致，并且表示蛋白质与 SDS 页被分析。50 kD 蛋白质特殊在 E 被表示。关口 i BL21，和结果与期望一致，并且证明 Hsp22.4 基因在 E 被表示了。关口 i。我们的学习为进一步学习 sHSPs 蛋白质的功能做了一个基础。

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-HSE 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 ofsHSPs protein.