The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complex.

@article{Erbse2009TheCS,
  title={The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complex.},
  author={Annette H. Erbse and Joseph J. Falke},
  journal={Biochemistry},
  year={2009},
  volume={48 29},
  pages={6975-87}
}
The chemosensory pathway of bacterial chemotaxis forms a polar signaling cluster in which the fundamental signaling units, the ternary complexes, are arrayed in a highly cooperative, repeating lattice. The repeating ternary units are composed of transmembrane receptors, histidine-kinase CheA, and coupling protein CheW, but it is unknown how these three core proteins are interwoven in the assembled ultrasensitive lattice. Here, to further probe the nature of the lattice, we investigate its… CONTINUE READING

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