| Issue |
E3S Web Conf.
Volume 185, 2020
2020 International Conference on Energy, Environment and Bioengineering (ICEEB 2020)
|
|
|---|---|---|
| Article Number | 04058 | |
| Number of page(s) | 3 | |
| Section | Chemical Engineering and Food Biotechnology | |
| DOI | https://doi.org/10.1051/e3sconf/202018504058 | |
| Published online | 01 September 2020 | |
Expression of recombinant mouse spastin in E. coli
School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, 300072, China
* Corresponding author: lwyj0416@163.com
Mutations of the gene SPAST that encodes a microtubule severing enzyme, spastin, are the most frequent cause of Hereditary spastic paraplegia (HSP) disease. HSP is heterogeneous group of inherited neurodegenerative disorders characterized predominantly by progressive lower limb spasticity and weakness. Spastin belongs ATPase associated with various cellular activities (AAA) protein family and catalyzes microtubule severing. Spastin in mouse and human are highly identical in protein sequence and several spastin mutation models in mice have been generated in order to evaluate the significance of spastin loss-of-function in mammals. Expression and purification of spastin and the mutant variants determined in patients will facilitate the structure-function relationship study of spastin. Here I systemically optimized the expression condition of a truncated version of mouse spastin in E. coli. The recombinant protein and a mutant were further purified for ATPase activity assay.
© The Authors, published by EDP Sciences, 2020
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