Application of SGT1-Hsp90 chaperone complex for soluble expression of NOD1 LRR domain in E. coli
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- 作者：Tae-Joon Hong ; Ji-Sook Hahn ; hahnjs@snu.ac.kr" class="auth_mail" title="E-mail the corresponding author
- 关键词：Nucleotide-binding oligomerization domain protein 1 (NOD1) ; Leucine-rich repeat (LRR) ; Suppressor of G2 allele of skp1 (SGT1) ; Heat shock protein 90 kDa (Hsp90) ; Soluble expression
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2016
- 出版时间：30 September 2016
- 年：2016
- 卷：478
- 期：4
- 页码：1647-1652
- 全文大小：810 K
文摘
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The NOD1 LRR domain was solubilized by SGT1 fusion in E. coli.
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The coexpression of HSP90 stabilized the SGT1-NOD1 LRR fusion protein.
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Several optimizations could enhance the expression level of the fusion protein.