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Bacterial sensor evolved by decreasing complexity.

Elizabet Monteagudo-Cascales1, José A Gavira2, Jiawei Xing3

  • 1Department of Biotechnology and Environmental Protection, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, Granada 18008, Spain.

Proceedings of the National Academy of Sciences of the United States of America
|January 29, 2025
PubMed
Summary
This summary is machine-generated.

Bacterial receptors use Cache domains to sense signals. Researchers found that formate recognition in a double-domain receptor (dCache) is similar to single-domain receptors (sCache), suggesting evolution by simplification.

Keywords:
chemotaxisevolutionreceptorsignal transduction

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Bacterial receptors utilize ligand-binding domains (LBDs) to detect environmental signals, influencing cellular processes.
  • Cache domains represent a widespread family of LBDs in bacteria, archaea, and eukaryotes, crucial for extracytosolic signal detection.
  • Cache domains exist as single (sCache) or double (dCache) structural modules, with the function of dCache domains being less understood.

Purpose of the Study:

  • To investigate the function and structural basis of formate recognition by the PacF chemoreceptor's dCache domain in *Pectobacterium atrosepticum*.
  • To explore the evolutionary relationship between dCache and sCache domains in formate sensing.
  • To elucidate the molecular mechanisms of ligand binding in both sCache and dCache domains.

Main Methods:

  • Identification and characterization of the PacF chemoreceptor and its role in chemoattraction.
  • High-resolution structural determination of formate-bound sCache and dCache domain family members.
  • Comparative analysis of ligand-binding mechanisms across different Cache domain architectures.

Main Results:

  • The PacF chemoreceptor recognizes formate at the membrane-distal module of its dCache domain, mediating chemoattraction.
  • A family of formate-specific sCache domains has evolved from dCache domains through the loss of the membrane-proximal module.
  • Despite low sequence identity, sCache and dCache domains exhibit highly similar molecular bases for formate binding.

Conclusions:

  • The membrane-proximal module in dCache domains may not be essential for ligand binding, potentially explaining its evolutionary loss.
  • Evolutionary reduction in complexity, exemplified by the transition from dCache to sCache domains, contributes to functional diversity in bacterial receptors.
  • This study enhances understanding of bacterial signal perception and the evolutionary strategies shaping receptor diversity.