A hydrophobic protein sequence can override a nuclear localization signal independently of protein context.

Abstract

Simian virus 40 T antigen is specifically targeted to the nucleus by the signal Pro-Lys-Lys-128-Lys-Arg-Lys-Val. We have previously described the isolation of a simian virus 40 T-antigen mutant, 676FS, which retains a wild-type nuclear localization signal but fails to accumulate properly in the nucleus and interferes with the nuclear localization of heterologous proteins. Here we report that the hydrophobic carboxy-terminal sequence novel to 676FS T antigen overrides the nuclear localization signal if fused to other proteins, thereby anchoring the proteins in the cytoplasm. We discuss possible mechanisms by which missorting of such a fusion protein could interfere with the nuclear transport of heterologous proteins.

Cite this paper

@article{Zee1991AHP, title={A hydrophobic protein sequence can override a nuclear localization signal independently of protein context.}, author={Kimberly J Van Zee and Fritz Appel and Ellen Fanning}, journal={Molecular and cellular biology}, year={1991}, volume={11 10}, pages={5137-46} }