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Fig. 5 | BMC Biotechnology

Fig. 5

From: Increased stable integration efficiency in CHO cells through enhanced nuclear localization of Bxb1 serine integrase

Fig. 5

Co-expression of proteins involved in the translocation of proteins into the nucleus. (A) Schematic illustration of the genetic construct expressing both Bxb1–NPLCx2 and Importin α, Importin ß, RanGTP, RCC1 or RanGAP. The two proteins were separated by GS linker, furin clevage site and T2A peptide. (B) Illustration of the translocation process of proteins into the nucleus [20]. Importin α interacts with importin ß through IBB (Importin-ß-binding) domain (orange block), exposing the binding cavity of importin α, allowing the binding of NLS sequence to it. The ternary complex is then translocated into the nucleus where binding of RanGTP to importin ß causes dissociation of the ternary complex. Subsequently, importin α binds to exportin complex composed of CAS and RanGTP, and the complex is transported out from the nucleus. The exportin complex is dissociated in the cytoplasm by Ran GAP, converting Ran-GTP to RanGDP. Ran-GDP is converted back to the active Ran-GTP form in the nucleus by regulator of chromosome condensation 1 (RCC1) protein (not shown in the figure)

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