Eliminating a set of four penicillin binding proteins triggers the Rcs phosphorelay and Cpx stress responses in Escherichia coli.

@article{Evans2013EliminatingAS,
  title={Eliminating a set of four penicillin binding proteins triggers the Rcs phosphorelay and Cpx stress responses in Escherichia coli.},
  author={Kerry L Evans and Suresh Kannan and Gang Li and Miguel de Pedro and Kevin D Young},
  journal={Journal of bacteriology},
  year={2013},
  volume={195 19},
  pages={
          4415-24
        }
}
Penicillin binding proteins (PBPs) are responsible for synthesizing and modifying the bacterial cell wall, and in Escherichia coli the loss of several nonessential low-molecular-weight PBPs gives rise to abnormalities in cell shape and division. To determine whether these proteins help connect the flagellar basal body to the peptidoglycan wall, we surveyed a set of PBP mutants and found that motility in an agar migration assay was compromised by the simultaneous absence of four enzymes: PBP4… CONTINUE READING

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