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Research Article

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

K van Zee, F Appel, E Fanning
K van Zee
Institute for Biochemistry, Munich, Germany.
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F Appel
Institute for Biochemistry, Munich, Germany.
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E Fanning
Institute for Biochemistry, Munich, Germany.
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DOI: 10.1128/MCB.11.10.5137
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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.

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A hydrophobic protein sequence can override a nuclear localization signal independently of protein context.
K van Zee, F Appel, E Fanning
Molecular and Cellular Biology Oct 1991, 11 (10) 5137-5146; DOI: 10.1128/MCB.11.10.5137

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A hydrophobic protein sequence can override a nuclear localization signal independently of protein context.
K van Zee, F Appel, E Fanning
Molecular and Cellular Biology Oct 1991, 11 (10) 5137-5146; DOI: 10.1128/MCB.11.10.5137
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