VirB6 and VirB10 from the Brucella type IV secretion system interact via the N-terminal periplasmic domain of VirB6

FEBS Lett. 2015 Jul 8;589(15):1883-9. doi: 10.1016/j.febslet.2015.05.051. Epub 2015 Jun 9.

Abstract

Type IV secretion systems are multi-protein complexes that transfer macromolecules across the cell envelope of bacteria. Identifying the sites of interaction between the twelve proteins (VirB1-VirB11 and VirD4) that form these complexes is key to understanding their assembly and function. We have here used phage display, bacterial two-hybrid and fluorescence-based interaction assays to identify an N-terminal domain of the inner membrane protein VirB6 as a site of interaction with the envelope-spanning VirB10 protein. Our results are consistent with the notion that VirB6 acts in concert with VirB10 as well as with VirB8 during secretion system assembly and function.

Keywords: Bacterial virulence; Membrane protein; Protein–protein interaction; Type IV secretion system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacteriophages / genetics
  • Binding Sites
  • Brucella / metabolism*
  • Green Fluorescent Proteins / genetics
  • Molecular Sequence Data
  • Periplasm / metabolism*
  • Spectrometry, Fluorescence
  • Two-Hybrid System Techniques

Substances

  • Bacterial Proteins
  • Green Fluorescent Proteins