Localisation of a family of complex-forming β-barrels in the T. vaginalis hydrogenosomal membrane

FEBS Lett. 2012 Nov 16;586(22):4038-45. doi: 10.1016/j.febslet.2012.10.004. Epub 2012 Oct 13.

Abstract

Crucial to organellogenesis was the development of membrane translocases responsible for delivering proteins to new cellular compartments. This investigation examines the Trichomonas vaginalis hydrogenosome, a mitochondrially derived organelle. We identify an expanded family of putative β-barrel proteins (THOM A-I) comprising nine related sequences. Sub-cellular localisation by immunofluorescence and biochemical fractionation is consistent with THOMs being localised to the hydrogenosomal membrane. Native gel electrophoresis and chemical cross-linking support the ability of THOM proteins to be components of membrane-bound oligomeric protein complexes, consistent with a role in protein translocation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Immunoprecipitation
  • Intracellular Membranes / metabolism*
  • Membrane Transport Proteins / classification
  • Membrane Transport Proteins / genetics
  • Membrane Transport Proteins / metabolism*
  • Microscopy, Confocal
  • Multiprotein Complexes / metabolism
  • Organelles / metabolism*
  • Phylogeny
  • Protein Binding
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Transfection
  • Trichomonas vaginalis / genetics
  • Trichomonas vaginalis / metabolism*

Substances

  • Membrane Transport Proteins
  • Multiprotein Complexes
  • Protozoan Proteins