Two independent peroxisomal targeting signals in catalase A of Saccharomyces cerevisiae

@article{Kragler1993TwoIP,
  title={Two independent peroxisomal targeting signals in catalase A of Saccharomyces cerevisiae},
  author={Friedrich Kragler and A Langeder and J Raupachova and Maximilian Binder and Andreas Hartig},
  journal={The Journal of Cell Biology},
  year={1993},
  volume={120},
  pages={665 - 673}
}
In contrast to many other peroxisomal proteins catalase A contains at least two peroxisomal targeting signals each sufficient to direct reporter proteins to peroxisomes. One of them resides at the extreme carboxy terminus constituting a new variant of this signal, -SSNSKF, not active in monkey kidney cells (Gould, S. J., G. A. Keller, N. Hosken, J. Wilkinson, and S. Subramani 1989. J. Cell Biol. 108:1657-1664). However, this signal is completely dispensable for import of catalase A itself. In… CONTINUE READING

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The carboxylterminal tripeptide Ala-Lys-Ile is essential for targeting Candida tropicalis trifunctional enzyme to yeast peroxisomes

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