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Imidazole as a Small Molecule Analogue in Two-Component Signal Transduction.

Stephani C Page1, Ruth E Silversmith2, Edward J Collins1,2

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Summary
This summary is machine-generated.

Imidazole acts as a rudimentary histidine-containing phosphotransfer (Hpt) domain in two-component signal transduction systems. It facilitates phosphotransfer in artificial phosphorelays, revealing insights into the response regulator

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Two-component signal transduction systems (TCSs) regulate cellular responses via phosphotransfer.
  • Canonical TCSs involve His → Asp phosphotransfer; phosphorelays add Asp → His phosphotransfer using histidine-containing phosphotransfer (Hpt) domains.
  • Response regulators (RRs) possess the catalytic core for His → Asp phosphotransfer.

Purpose of the Study:

  • To investigate imidazole's potential role as a rudimentary Hpt domain in phosphotransfer.
  • To elucidate the mechanism of phosphotransfer involving imidazole and RRs.
  • To understand the structural and kinetic basis of imidazole's interaction with RRs.

Main Methods:

  • Biochemical assays to measure phosphotransfer rates between imidazole, RRs, and monophosphoimidazole (MPI).
  • X-ray crystallography to determine the structure of an activated RR·imidazole complex.
  • Kinetic analysis using chimeric RRs to assess the role of active site residues.

Main Results:

  • Imidazole functions as a nucleophile, attacking phosphorylated RRs (RR-P) to form MPI and unphosphorylated RR.
  • Phosphotransfer from RR-P to imidazole requires an intact RR active site, indicating RR's catalytic role.
  • Imidazole acts as a shuttle in artificial phosphorelays, transferring phosphoryl groups between RRs.
  • The crystal structure shows imidazole oriented similarly to Hpt-His in the RR active site.
  • Interactions with nonconserved RR residues modulate RR-P reactivity with imidazole versus water.
  • Kinetic data suggest RR active site influences phosphotransfer preferences, similar to Hpt domains.

Conclusions:

  • Imidazole exhibits characteristics of a rudimentary Hpt domain, participating in Asp → His phosphotransfer.
  • The RR active site is crucial for catalyzing phosphotransfer with imidazole.
  • Imidazole can be utilized in artificial phosphorelays, offering a tool for studying TCS mechanisms.
  • Structural and kinetic data provide mechanistic insights into phosphotransfer in TCSs and phosphorelays.