Application of SGT1-Hsp90 chaperone complex for soluble expression of NOD1 LRR domain in E. coli
作者： Tae-Joon Hong , Ji-Sook Hahn
DOI: 10.1016/J.BBRC.2016.08.174
关键词:
摘要: NOD1 is an intracellular sensor of innate immunity which related to a number inflammatory diseases. known be difficult express and purify for structural biochemical studies. Based on the fact that Hsp90 its cochaperone SGT1 are necessary stabilization activation in mammals, was chosen as fusion partner leucine-rich repeat (LRR) domain soluble expression Escherichia coli. Fusion human (hSGT1) LRR significantly enhanced solubility, protein stabilized by coexpression mouse Hsp90α. The level hSGT1-NOD1 further supplementation rare codon tRNAs exchange antibiotic marker genes.
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