Communication of ClpXP protease hypersensitivity to bacteriophage Mu repressor isoforms.

@article{Welty1997CommunicationOC,
  title={Communication of ClpXP protease hypersensitivity to bacteriophage Mu repressor isoforms.},
  author={D J Welty and Jessica M. Jones and Hiroshi Nakai},
  journal={Journal of molecular biology},
  year={1997},
  volume={272 1},
  pages={31-41}
}
The immunity repressor (Rep) of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. Although Rep is stable in vivo, an altered immunity repressor (Vir) encoded by virulent, trans-dominant Mu mutants is rapidly degraded by Escherichia coli ClpXP protease. Rep and Vir are degraded at approximately the same maximal velocity (Vmax) by ClpXP, but the Km for Rep (3.6 microM) is over 20-fold higher than the Km for Vir (0.15… CONTINUE READING