Lon and Clp family proteases and chaperones share homologous substrate-recognition domains.

@article{Smith1999LonAC,
  title={Lon and Clp family proteases and chaperones share homologous substrate-recognition domains.},
  author={Catherine K Smith and Tania A. Baker and Robert T. Sauer},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 12},
  pages={6678-82}
}
Lon protease and members of the Clp family of molecular chaperones and protease regulatory subunits contain homologous regions with properties expected for substrate-binding domains. Fragments corresponding to these sequences are stably and independently folded for Lon, ClpA, and ClpY. The corresponding regions from ClpB and ClpX are unstable. All five fragments exhibit distinct patterns of binding to three proteins that are protease substrates in vivo: the heat shock transcription factor… CONTINUE READING

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