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Related Experiment Video

Updated: Nov 15, 2025

Bacterial Leaf Infiltration Assay for Fine Characterization of Plant Defense Responses using the Arabidopsis thaliana-Pseudomonas syringae Pathosystem
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Structural basis for a bacterial Pip system plant effector recognition protein.

Shukun Luo1, Bruna G Coutinho2, Prikshat Dadhwal1

  • 1Department of Biological Sciences, Columbia University, New York, NY 10027.

Proceedings of the National Academy of Sciences of the United States of America
|March 2, 2021
PubMed
Summary

Researchers discovered a plant molecule, HEHEAA, that controls bacterial gene regulation in plant-associated bacteria. This molecule binds to a specific protein, influencing bacterial interactions with plants and their virulence.

Keywords:
PopulusPseudomonas signalingsubstrate-binding protein

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Plant Pathology

Background:

  • Plant-associated proteobacteria utilize LuxR family transcription factors, known as PipR subfamily members, which are crucial for bacterial-plant interactions and virulence.
  • Understanding the regulatory mechanisms of these bacterial proteins is key to deciphering plant-microbe communication and developing strategies to control plant diseases.

Purpose of the Study:

  • To identify and characterize small molecules that act as effectors for PipR-mediated gene regulation.
  • To elucidate the molecular basis of how PipR systems recognize and respond to plant-derived factors.
  • To investigate the structural and functional basis of effector binding to substrate-binding proteins (SBPs) associated with PipR systems.

Main Methods:

  • Identification of N-(2-hydroxyethyl)-2-(2-hydroxyethylamino) acetamide (HEHEAA) as a PipR effector in Pseudomonas GM79.
  • Crystallization and structural analysis of a HEHEAA-responsive SBP in its free and HEHEAA-bound states.
  • Structure-based mutational analysis to confirm the HEHEAA binding mode and assess cross-reactivity with SBPs from other Pseudomonas species.

Main Results:

  • HEHEAA binds to the periplasmic substrate-binding protein (SBP) of an ATP-binding cassette-type active transport system, modulating PipR activity.
  • Structural data revealed that the SBP possesses a closed conformation with a cavity accommodating HEHEAA via hydrogen bonds and specific residue interactions, but not larger peptides.
  • A closely related SBP from Pseudomonas syringae pv tomato DC3000 did not bind HEHEAA, but a single amino acid substitution enabled weak binding, suggesting effector specificity.

Conclusions:

  • HEHEAA is a novel effector that regulates PipR-mediated gene expression in plant-associated bacteria.
  • The structure of the HEHEAA-bound SBP provides insights into the molecular recognition mechanism of this effector.
  • PipR-associated SBPs exhibit effector specificity, implying diverse roles in mediating interactions between different plant-associated bacteria and their hosts.