Assembly and targeting of secretins in the bacterial outer membrane

Int J Med Microbiol. 2019 Nov;309(7):151322. doi: 10.1016/j.ijmm.2019.06.002. Epub 2019 Jun 19.

Abstract

In Gram-negative bacteria, secretion of toxins ensure the survival of the bacterium. Such toxins are secreted by sophisticated multiprotein systems. The most conserved part in some of these secretion systems are components, called secretins, which form the outer membrane ring in these systems. Recent structural studies shed some light on the oligomeric organization of secretins. However, the mechanisms by which these proteins are targeted to the outer membrane and assemble there into ring structures are still not fully understood. This review discusses the various species-specific targeting and assembly pathways that are taken by secretins in order to form their functional oligomers.

Keywords: BAM complex; Gram-negative bacteria; Periplasmic chaperones; Secretins.

Publication types

  • Review

MeSH terms

  • Bacterial Outer Membrane / chemistry
  • Bacterial Outer Membrane / metabolism*
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Secretion Systems / chemistry
  • Bacterial Secretion Systems / metabolism
  • Gram-Negative Bacteria / chemistry
  • Gram-Negative Bacteria / metabolism
  • Membrane Transport Proteins / chemistry*
  • Membrane Transport Proteins / metabolism*
  • Models, Biological
  • Models, Molecular
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism
  • Protein Multimerization
  • Protein Transport

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Secretion Systems
  • Membrane Transport Proteins
  • Molecular Chaperones