AI Article Synopsis
- The production of cysteine-rich proteins in E. coli is challenging due to low yield and poor folding efficiency.
- Researchers created expression vectors that fuse Buthus martensii Karsch insect toxin to a specific intein to improve protein production.
- The placement of the His(6) tag is crucial; one configuration produces insoluble protein, while another yields soluble and properly folded insect toxin.
Article Abstract
The low yield and poor folding efficiency in vivo of soluble and active recombinant cysteine-rich proteins expressed in Escherichia coli are a major challenge for large-scale protein production and purification. Expression vectors containing Buthus martensii Karsch insect toxin (BmK IT) fused to the C terminus of the intein Ssp DnaB were constructed in an attempt to overcome this problem. Following purification and intein self-cleavage, the fusion protein His(6)-intein-IT produced insoluble BmK IT, while intein-IT-His(6) generated soluble and properly folded BmK IT. This result indicated that the positioning of the His(6) tag has a key role in the production of soluble and functional BmK IT.
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| http://dx.doi.org/10.1016/j.pep.2008.01.009 | DOI Listing |
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