A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.

@article{Westphal2012ATA,
  title={A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.},
  author={Kai Westphal and Sina Langklotz and Nikolas Thomanek and Franz Narberhaus},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 51},
  pages={42962-71}
}
Proteolysis is a universal strategy to rapidly adjust the amount of regulatory and metabolic proteins to cellular demand. FtsH is the only membrane-anchored and essential ATP-dependent protease in Escherichia coli. Among the known functions of FtsH are the control of the heat shock response by proteolysis of the transcription factor RpoH (σ(32)) and its essential role in lipopolysaccharide biosynthesis by degradation of the two key enzymes LpxC and KdtA. Here, we identified new FtsH substrates… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 15 extracted citations

How Is Fe-S Cluster Formation Regulated?

Annual review of microbiology • 2015
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…