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Mirror proteorhodopsins.

Ivan S Okhrimenko1, Kirill Kovalev2, Lada E Petrovskaya3

  • 1Research Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.

Communications Chemistry
|May 2, 2023
PubMed
Summary

Researchers discovered novel bacterial rhodopsins, termed "mirror proteorhodopsins," that pump protons at acidic pH. These unique proton pumps are inhibited by zinc and found in various bacteria, including pathogens.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Proteorhodopsins (PRs) are the largest family of light-driven outward proton pumps in bacteria.
  • A gap in knowledge existed regarding bacterial rhodopsins functioning at acidic pH, despite diverse bacterial environments.

Purpose of the Study:

  • To describe novel bacterial rhodopsins operating as outward proton pumps at acidic pH.
  • To characterize the structure-function relationship of these new rhodopsins.

Main Methods:

  • Comprehensive function-structure studies of a representative rhodopsin from Sphingomonas paucimobilis (SpaR).
  • Analysis of proton translocation pathways and inhibition by zinc.

Main Results:

  • Discovery of a new clade of proton pumping rhodopsins, named "mirror proteorhodopsins."
  • SpaR exhibits a unique cavity/gate architecture for proton translocation, distinct from known PRs.
  • Proton pumping by mirror proteorhodopsins is inhibited by millimolar zinc concentrations.
  • Mirror proteorhodopsins are prevalent in opportunistic pathogens, plant growth-promoting, and zinc-solubilizing bacteria.

Conclusions:

  • Mirror proteorhodopsins represent a conceptually new class of bacterial proton pumps.
  • Their unique structural and functional properties, including zinc inhibition, warrant further investigation.
  • These rhodopsins have potential applications in optogenetics and are relevant to bacterial adaptation and pathogenesis.