期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 478, 期 4, 页码 1647-1652出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.08.174
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
资金
- Priority Research Centers Program Grant from National Research Foundation of Korea - Ministry of Education, Science and Technology [2011-0031388]
NOD1 is an intracellular sensor of innate immunity which is related to a number of inflammatory diseases. NOD1 is known to be difficult to express and purify for structural and biochemical studies. Based on the fact that Hsp90 and its cochaperone SGT1 are necessary for the stabilization and activation of NOD1 in mammals, SGT1 was chosen as a fusion partner of the leucine-rich repeat (LRR) domain of NOD1 for its soluble expression in Escherichia coli. Fusion of human SGT1 (hSGT1) to NOD1 LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90a. The expression level of hSGT1-NOD1 LRR was further enhanced by supplementation of rare codon tRNAs and exchange of antibiotic marker genes. (C) 2016 Elsevier Inc. All rights reserved.
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