| 초록 |
Escherichia coli Protein P is resistant to proteolitic cleavage. The strong stability and rigidity of Protein P is noticeable since all fusion partners need the abilities to work as solubility enhancers. Protein P consists of two domains, C-domain and N-domain. The two domains are structurally similar, but C-domain is not able to make correct folding alone. N-domain induces correct folding of C-domain, and they make solid globular conformation. When Protein P is used as a fusion partner of recombinant proteins which are aggregated to inclusion bodies in E.coli cytoplasm, the solubility of the proteins is dramatically increased by the post priming effect of Protein P. Separated N-domain, moreover, has great ability in enhancing the solubility of all recombinant proteins fused. These demonstrate that E.coli Protein P can be used as a universal solubility tag for aggregation-susceptible non-homologous proteins in E. coli cytoplasm. |
