Regulation of a nuclear export signal by an adjacent inhibitory sequence: the effector domain of the influenza virus NS1 protein.

@article{Li1998RegulationOA,
  title={Regulation of a nuclear export signal by an adjacent inhibitory sequence: the effector domain of the influenza virus NS1 protein.},
  author={Yingjie Li and Yoshihiko Yamakita and Robert Krug},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 9},
  pages={4864-9}
}
In the cell nucleus the NS1 protein of influenza A virus inhibits both pre-mRNA splicing and the nuclear export of mRNAs. Both the RNA-binding and effector domains of the protein are required for these nuclear functions. Here we demonstrate that the NS1 protein has a latent nuclear export signal (NES) that is located at the amino end of the effector domain. In uninfected, transfected cells the NS1 protein is localized in the nucleus because the NES is specifically inhibited by the adjacent… CONTINUE READING

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Mentioned Connections BETA
Substitution of alanine residues for specific amino acids in the adjacent sequence abrogates its inhibitory activity , thereby unmasking the NES and causing the full - length NS1 protein to be localized to the cytoplasm .
Substitution of alanine residues for specific amino acids in the adjacent sequence abrogates its inhibitory activity , thereby unmasking the NES and causing the full - length NS1 protein to be localized to the cytoplasm .
Substitution of alanine residues for specific amino acids in the adjacent sequence abrogates its inhibitory activity , thereby unmasking the NES and causing the full - length NS1 protein to be localized to the cytoplasm .
Amino AcidsChemical structure ofAlanine
Substitution of alanine residues for specific amino acids in the adjacent sequence abrogates its inhibitory activity , thereby unmasking the NES and causing the full - length NS1 protein to be localized to the cytoplasm .
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