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<i>In vivo</i> tests of the <i>E. coli</i> TonB system working model-interaction of ExbB with unknown proteins, identification of TonB-ExbD transmembrane heterodimers and PMF-dependent ExbD structures.

bioRxiv : the preprint server for biology·2024
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The Intrinsically Disordered Region of ExbD Is Required for Signal Transduction.

Dale R Kopp1, Kathleen Postle2

  • 1Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania, USA.

Journal of Bacteriology
|January 15, 2020
PubMed
Summary
This summary is machine-generated.

The TonB system uses ExbB, ExbD, and TonB proteins to transport nutrients across bacterial outer membranes. This study reveals a disordered ExbD domain and a key motif essential for signal transduction in this energy transfer process.

Keywords:
ExbBExbDTonBconserved binding motifconserved motifenergy transductionintrinsic disordersignal transduction

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The TonB system is crucial for nutrient uptake in Gram-negative bacteria, utilizing inner membrane proton motive force (PMF) to power outer membrane transporters.
  • Integral membrane proteins ExbB, ExbD, and TonB form a complex to transduce energy.
  • Previous studies indicated a role for a disordered ExbD domain in PMF-dependent TonB interaction.

Purpose of the Study:

  • To investigate the function of the ExbD disordered domain in the TonB energy transduction system.
  • To identify protein complexes formed by ExbD during the energy transduction cycle.
  • To determine the role of a conserved motif within the ExbD disordered domain.

Main Methods:

  • Utilized *in vivo* photo-cross-linking with sequential pBpa substitutions in the ExbD disordered domain.
  • Analyzed captured ExbD complexes, including heterodimers and homodimers.
  • Investigated the impact of deletions and substitutions within the conserved motif on signal transduction.

Main Results:

  • Captured five distinct ExbD complexes, including novel ExbB-ExbD heterodimers and a PMF-independent ExbD-TonB interaction.
  • Demonstrated the dynamic nature of ExbD interactions throughout the energy transduction cycle.
  • Identified a conserved motif (V45, V47, L49, P50) essential for signal transduction to TonB and the ExbD C-terminal domain.

Conclusions:

  • The ExbD disordered domain plays a dynamic role in the TonB energy transduction cycle.
  • A conserved motif within this domain is critical for relaying signals to TonB and other ExbD regions.
  • This motif's function is essential for configuring TonB to interact with outer membrane transporters, highlighting its importance in bacterial physiology and virulence.