The interplay of ClpXP with the cell division machinery in Escherichia coli.

@article{Camberg2011TheIO,
  title={The interplay of ClpXP with the cell division machinery in Escherichia coli.},
  author={Jodi L Camberg and Joel R. Hoskins and Sue Wickner},
  journal={Journal of bacteriology},
  year={2011},
  volume={193 8},
  pages={1911-8}
}
ClpXP is a two-component protease composed of ClpX, an ATP-dependent chaperone that recognizes and unfolds specific substrates, and ClpP, a serine protease. One ClpXP substrate in Escherichia coli is FtsZ, which is essential for cell division. FtsZ polymerizes and forms the FtsZ ring at midcell, where division occurs. To investigate the role of ClpXP in cell division, we examined the effects of clpX and clpP deletions in several strains that are defective for cell division. Together, our… CONTINUE READING

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