Part:BBa_K4414003
NES
This nuclear export signal（NES）directs the protein out of the nucleus.
Usage and Biology
Regulating the output of many proteins from the nucleus depends on the presence of a nuclear export signal(NES) consisting of leucine-rich amino acids.[1][2]. The shuttle receptor that appears to bind to the NES sequence and function in the protein output from the nucleus to the cytoplasm is CRM1 (chromosomal region maintenance)/export protein 1.[3] CRM1 binds to Ran GTPase and interacts with the nucleoporous components to translocate NES-containing proteins to the cytoplasm.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Functional characterization
We can connect NES to EGFP and observe the location of fluorescent proteins to verify the function of NES.In order to test the effect of NES on background value reduction, we compared the SEAP characterization effect of components without NES with those adding NES.
Figure 2.The picture on the left is Bright-field cell diagram, the picture in the middle is fluorescence diagram, and the picture on the right is merge diagram.
Reference
[1].Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W., & Lührmann, R. (1995). The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell, 82(3), 475–483. https://doi.org/10.1016/0092-8674(95)90436-0 [2].Fornerod, M., Ohno, M., Yoshida, M., & Mattaj, I. W. (1997). CRM1 is an export receptor for leucine-rich nuclear export signals. Cell, 90(6), 1051–1060. https://doi.org/10.1016/s0092-8674(00)80371-2 [3].Richards, S. A., Carey, K. L., & Macara, I. G. (1997). Requirement of guanosine triphosphate-bound ran for signal-mediated nuclear protein export. Science (New York, N.Y.), 276(5320), 1842–1844. https://doi.org/10.1126/science.276.5320.1842
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