The ATPase domain of HscC (DnaK homolog) is essential for interfering sigma70 activity in E. coli.

@article{Arifuzzaman2004TheAD,
  title={The ATPase domain of HscC (DnaK homolog) is essential for interfering sigma70 activity in E. coli.},
  author={Mohammad Arifuzzaman and Taku Oshima and Hirotada Mori},
  journal={FEMS microbiology letters},
  year={2004},
  volume={230 1},
  pages={99-104}
}
HscC, a DnaK homolog in Escherichia coli, consists of adenosine triphosphatase (ATPase), substrate-binding and C-terminal domains. Overexpression of HscC markedly inhibits growth of host cell and reduces the sigma(70)-dependent promoter activity presumably by forming a complex with sigma(70). To identify the region(s) of HscC responsible for growth inhibition and complex formation with sigma(70), domain swapping experiments were carried out between DnaK and HscC. Thus the chimeric proteins… CONTINUE READING

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