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Structural basis for selective GABA binding in bacterial pathogens.

Sara Planamente1, Samuel Mondy, Florence Hommais

  • 1Institut des Sciences du Végétal, CNRS, avenue de la terrasse, 91198, Gif-sur-Yvette, France.

Molecular Microbiology
|October 10, 2012
PubMed
Summary
This summary is machine-generated.

Researchers identified a novel gamma-aminobutyric acid (GABA) sensor, Atu4243, in Agrobacterium tumefaciens. This discovery reveals the structural basis for bacterial GABA sensing and its role in host-pathogen interactions.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Gamma-aminobutyric acid (GABA) functions as a crucial intercellular signal in eukaryotes and an interspecies signal in host-microbe interactions.
  • The structural details of selective eukaryotic GABA receptors and bacterial GABA sensors remain largely unknown.
  • Understanding these structures is vital for deciphering GABA's role in biological communication.

Purpose of the Study:

  • To identify and characterize a selective GABA-binding protein in the plant pathogen Agrobacterium tumefaciens.
  • To elucidate the structure of the GABA-bound protein and its interaction with GABA.
  • To explore the functional implications of GABA sensing in bacterial pathogenesis and communication.

Main Methods:

  • Protein identification and characterization of a GABA-binding protein (Atu4243) in Agrobacterium tumefaciens.
  • Construction and analysis of an atu4243 mutant to assess GABA transport and regulated functions.
  • X-ray crystallography to determine the 1.28 Å structure of GABA-bound Atu4243.
  • Site-directed mutagenesis to validate the role of key residues (Arg(203), Asp(226)) in GABA binding and signaling.
  • Genomic database exploration to identify orthologues of Atu4243.

Main Results:

  • Identification of Atu4243 as a selective GABA-binding protein in Agrobacterium tumefaciens.
  • The atu4243 mutant exhibited defects in GABA transport and GABA-regulated functions, including plant aggressiveness and quorum-sensing signal degradation.
  • The high-resolution structure revealed GABA in a novel conformation, interacting with Arg(203) and Asp(226).
  • Mutational analysis confirmed the critical roles of Arg(203) and Asp(226) in GABA binding and signaling.
  • The GABA analogue TACA acted as an antagonist, suggesting similarities with mammalian GABA(C) receptors.
  • Orthologues of Atu4243 were found in various pathogenic and symbiotic proteobacteria.

Conclusions:

  • This study establishes the first structural basis for a selective bacterial GABA sensor, Atu4243.
  • The findings highlight the importance of GABA-mediated communication in Agrobacterium tumefaciens pathogenesis and interspecies interactions.
  • The identified structural features and conserved orthologues offer potential for understanding and manipulating GABA signaling in diverse host-pathogen systems.