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Interdomain Linkers Regulate Histidine Kinase Activity by Controlling Subunit Interactions.

Zachary Maschmann1, Siddarth Chandrasekaran1,2, Teck Khiang Chua1

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York14850, United States.

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This summary is machine-generated.

Altering peptide linkers in bacterial CheA kinase affects its autophosphorylation activity. Linker flexibility and spacing, not sequence, control kinase domain proximity and substrate domain mobility, influencing regulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Bacterial chemoreceptors control histidine kinase CheA activity via poorly understood mechanisms.
  • Peptide linkers connecting CheA's kinase domains are critical for its regulation.

Purpose of the Study:

  • Investigate the role of peptide linkers (L3 and L4) in modulating Thermotoga maritima CheA activity.
  • Determine how linker modifications impact CheA autophosphorylation and domain dynamics.

Main Methods:

  • Engineered variants of Thermotoga maritima CheA with extended and altered L3 and L4 linkers.
  • Assessed nucleotide binding, CheW interactions, and autophosphorylation activity.
  • Utilized pulse-dipolar electron-spin resonance (ESR) with spin-labeled ATP analogues.

Main Results:

  • Linker extensions in CheA-LV1 reduced autophosphorylation ~50-fold but maintained WT-like binding.
  • Autophosphorylation required specific linker spacing and flexibility, favoring helical structures.
  • ESR data showed inverse correlation between P4 domain proximity and autophosphorylation activity.
  • Linkers influenced P1 substrate domain mobility despite spatial separation.

Conclusions:

  • CheA autophosphorylation is regulated by P4 domain interactions modulated by L3 and L4 linkers.
  • Linker-dependent domain dynamics and proximity are key to CheA activity.
  • This provides insights into how bacterial chemoreceptors regulate CheA kinase activity.