ArticleProtein expression and purification2027
Optimization of the recombinant overexpression and purification of human Nedd4-1 in Escherichia coli.
Article in Protein expression and purification, 2027. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The E3 ubiquitin ligase Nedd4-1 is a structurally complex, multidomain enzyme that plays a crucial role in maintaining proteostasis and regulating the cellular stress response. Nedd4-1's complex regulatory mechanism involves both intermolecular interactions (with upstream E2 conjugating enzymes and substrates) and intramolecular interactions that govern its function. Additionally, Nedd4-1 has received increased attention recently due to a small-molecule N-arylbenzimidazole 2 (NAB2) that prevents proteotoxicity and restores organelle trafficking associated with synucleopathies in a Nedd4-1-dependent manner. To study the enzymology of Nedd4-1, it is essential to employ recombinant Nedd4-1 in its native and untagged form to ensure high-fidelity biophysical characterization. In this study, we develop an efficient and optimized methodology for enhanced expression and purification of untagged active Nedd4-1 from E. coli over three affinity column steps. This strategy employs a nine-residue poly-histidine tag, glutathione S-transferase, and proteolytic cleavage with the TEV fusion protease, His
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