Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system

J Microbiol. 2019 Mar;57(3):185-194. doi: 10.1007/s12275-019-8520-1. Epub 2019 Feb 26.

Abstract

Tripartite efflux pumps and the type I secretion system of Gram-negative bacteria are large protein complexes that span the entire cell envelope. These complexes expel antibiotics and other toxic substances or transport protein toxins from bacterial cells. Elucidating the binary and ternary complex structures at an atomic resolution are crucial to understanding the assembly and working mechanism. Recent advances in cryoelectron microscopy along with the construction of chimeric proteins drastically shifted the assembly models. In this review, we describe the current assembly models from a historical perspective and emphasize the common assembly mechanism for the assembly of diverse tripartite pumps and type I secretion systems.

Keywords: cryo-electron microscopy; multidrug efflux pump; multidrug resistance; structure.

Publication types

  • Review

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Cryoelectron Microscopy
  • Drug Resistance, Bacterial*
  • Genes, MDR / genetics
  • Gram-Negative Bacteria / genetics
  • Gram-Negative Bacteria / physiology*
  • Membrane Transport Proteins / genetics
  • Membrane Transport Proteins / metabolism
  • Periplasmic Proteins / genetics
  • Periplasmic Proteins / metabolism
  • Protein Multimerization
  • Type I Secretion Systems / genetics
  • Type I Secretion Systems / metabolism*

Substances

  • Anti-Bacterial Agents
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Carrier Proteins
  • Membrane Transport Proteins
  • Periplasmic Proteins
  • Type I Secretion Systems