Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.

@article{Blackshear2003CharacteristicsOT,
  title={Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.},
  author={Perry J. Blackshear and Wi S. Lai and Elizabeth A. Kennington and Gary Brewer and Gerald M. Wilson and Xiaoju Guan and Pei Zhou},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 22},
  pages={19947-55}
}
Tristetraprolin (TTP) and its two known mammalian family members are tandem CCCH zinc finger proteins that can bind to AU-rich elements (AREs) in cellular mRNAs and destabilize those transcripts, apparently by initiating their deadenylation. Previous studies have shown that the approximately 70-amino acid tandem zinc finger domain of TTP is required and sufficient for RNA binding, and that the integrity of both zinc fingers is also required. However, little is known about the kinetics or… CONTINUE READING

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