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Kedar Puvar1, Aya M Saleh2, Ryan W Curtis1

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|March 26, 2020
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Summary
This summary is machine-generated.

Legionella pneumophila

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Classical ubiquitination involves three enzymes (E1-E2-E3).
  • Legionella pneumophila SidE effectors use NAD+ for ubiquitination.
  • This bacterial mechanism differs significantly from eukaryotic pathways.

Purpose of the Study:

  • To develop real-time assays for monitoring the two-step SidE effector mechanism.
  • To enable biochemical studies and inhibitor screening.
  • To facilitate discovery of similar enzymes in other organisms.

Main Methods:

  • Utilized fluorescent NAD+ analogues.
  • Employed synthetic substrate mimics.
  • Developed continuous assays for real-time monitoring.

Main Results:

  • Successfully monitored both steps of the SidE effector mechanism in real-time.
  • Demonstrated the utility of assays for inhibitor screening.
  • Showed assays can study enzymes reversing the modification.

Conclusions:

  • Developed novel continuous assays for SidE effector function.
  • These assays are valuable tools for biochemical studies and drug discovery.
  • The methodology aids in understanding and targeting bacterial post-translational modifications.