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A Selective Tether Recruits Activated Response Regulator CheB to Its Chemoreceptor Substrate.

Mingshan Li1, Xianjin Xu2,3,4, Xiaoqin Zou1,2,3,4

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Bacterial chemotaxis protein CheB (methylesterase/deamidase) is activated by phosphorylation and binding to a pentapeptide on chemoreceptors. This interaction enhances CheB

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Area of Science:

  • Microbiology and Molecular Biology
  • Biochemistry and Biophysics

Background:

  • Two-component signal transduction systems enable bacteria to sense and respond to environmental cues.
  • Response regulators, like CheB (methylesterase/deamidase), are crucial components, often acting as enzymes.
  • CheB activation involves phosphorylation and interaction with chemoreceptor pentapeptide motifs.

Purpose of the Study:

  • To investigate the interplay between CheB phosphorylation, pentapeptide binding, and substrate interaction.
  • To elucidate the mechanism of CheB regulation by its chemoreceptor target.

Main Methods:

  • Characterization of binding kinetics of CheB to Nanodisc-inserted chemoreceptor dimers.
  • Utilized a phosphorylation mimic to assess its effect on pentapeptide binding.
  • Employed molecular modeling to predict the pentapeptide-binding site on CheB.

Main Results:

  • A synergistic relationship was observed between CheB phosphorylation and pentapeptide binding.
  • Phosphorylation mimic enhanced pentapeptide binding, with the pentapeptide acting as a high-affinity tether.
  • The pentapeptide selectively binds phosphorylated CheB, stabilizing its active conformation.

Conclusions:

  • CheB activation is regulated by a novel mechanism involving selective tethering of the activated enzyme by its target.
  • Chemoreceptor pentapeptides act as selective tethers, recruiting and stabilizing the active conformation of CheB.
  • This highlights an active role for target molecules in regulating response regulator activity, a potentially widespread strategy in bacterial signaling.