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Related Experiment Videos

The IncP plasmid-encoded cell envelope-associated DNA transfer complex increases cell permeability

R Daugelavicius1, J K Bamford, A M Grahn

  • 1Department of Biosciences, Biocenter, University of Helsinki, Finland.

Journal of Bacteriology
|August 1, 1997
PubMed
Summary

This study quantifies mating pair formation (Mpf) complexes on bacterial cell surfaces. Mpf affects cell envelope permeability and ion transport, disassembling when ATP levels drop.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biophysics

Background:

  • IncP-type plasmids are broad-host-range conjugative plasmids crucial for horizontal gene transfer.
  • DNA translocation during conjugation requires DNA transfer-replication functions and mating pair formation (Mpf) systems.
  • The Mpf system, located in cell membranes, mediates DNA transport and functions as a receptor for IncP-specific phages like PRD1.

Purpose of the Study:

  • To quantify the number of Mpf complexes on the bacterial cell surface.
  • To investigate the biophysical effects of Mpf complexes on cell envelope properties and membrane potential.
  • To determine the stability of Mpf complexes in relation to intracellular ATP concentration.

Main Methods:

  • Phage receptor saturation technique was employed to quantify Mpf complexes.

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  • Electrochemical measurements were utilized to assess cell envelope permeability and ion transport.
  • A PRD1 adsorption assay was used to monitor Mpf complex disassembly under varying ATP conditions.

    • Main Results:

    • The Mpf complex significantly increases cell envelope permeability to lipophilic compounds and ATP.
    • Mpf complexes reduce the cell's ability to accumulate potassium ions (K+) but do not dissipate membrane voltage.
    • Decreased intracellular ATP concentration leads to rapid disassembly of the Mpf complex.

    Conclusions:

    • The Mpf complex plays a critical role in regulating cell envelope permeability and ion homeostasis during plasmid conjugation.
    • Mpf complex stability is directly dependent on intracellular ATP levels, suggesting an energy-dependent mechanism for its function and disassembly.
    • These findings provide insights into the biophysical properties and regulation of the Mpf system in IncP-type plasmid conjugation.