AI Article Synopsis

  • GABA (γ-Aminobutyric acid) acts as a signaling molecule in plants, especially during stress and interactions with harmful bacteria, but its mechanisms are not fully understood.
  • Researchers identified a GABA receptor named McpG in the plant-pathogenic bacterium Pseudomonas syringae pv. tabaci 6605 (Pta6605) and created a mutant lacking this receptor to study its role in GABA chemotaxis.
  • The findings showed that while Pta6605 normally responds to GABA, the ΔmcpG mutant lost this attraction and was less effective in causing disease in tobacco plants, indicating that GABA sensing is crucial for the bacterium's interaction with its host.

Article Abstract

γ-Aminobutyric acid (GABA) is a widely distributed non-proteinogenic amino acid that accumulates in plants under biotic and abiotic stress conditions. Recent studies suggested that GABA also functions as an intracellular signaling molecule in plants and in signals mediating interactions between plants and phytopathogenic bacteria. However, the molecular mechanisms underlying GABA responses to bacterial pathogens remain unknown. In the present study, a GABA receptor, named McpG, was conserved in the highly motile plant-pathogenic bacteria Pseudomonas syringae pv. tabaci 6605 (Pta6605). We generated a deletion mutant of McpG to further investigate its involvement in GABA chemotaxis using quantitative capillary and qualitative plate assays. The wild-type strain of Pta6605 was attracted to GABA, while the ΔmcpG mutant abolished chemotaxis to 10‍ ‍mM GABA. However, ΔmcpG retained chemotaxis to proteinogenic amino acids and succinic semialdehyde, a structural analog of GABA. Furthermore, ΔmcpG was unable to effectively induce disease on host tobacco plants in three plant inoculation assays: flood, dip, and infiltration inoculations. These results revealed that the GABA sensing of Pta6605 is important for the interaction of Pta6605 with its host tobacco plant.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7734410PMC
http://dx.doi.org/10.1264/jsme2.ME20114DOI Listing

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