Gene expression and molecular characterization of a chaperone protein HtpG from Bacillus licheniformis
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- 作者：Hui-Fen Loa ; 1 ; Bo-En Chenb ; 1 ; Min-Guan Linc ; Meng-Chun Chib ; Tzu-Fan Wangd ; catalpa0905@gmail.com" class="auth_mail" title="E-mail the corresponding author ; Long-Liu Linb ; llin@mail.ncyu.edu.tw" class="auth_mail" title="E-mail the corresponding author
- 关键词：Heat shock protein 90 ; Bacillus licheniformis ; ATPase activity ; Protein conformation ; Alkaline pH
- 刊名：International Journal of Biological Macromolecules
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：85
- 期：Complete
- 页码：179-191
- 全文大小：4179 K
文摘
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The putative HtpG gene of B. licheniformis is cloned and expressed in E. coli.
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The recombinant HtpG exists as a mixture of monomer, dimer and other oligomers in solution.
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The protein conformation is stable at higher temperatures under neutral pH, but is thermally sensitive at alkaline conditions.
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It also experiences a significant change in the molecular architecture upon the addition of ATP and certain concentrations of organic solvents.