A component of the mitochondrial outer membrane proteome of T. brucei probably contains covalent bound fatty acids

Exp Parasitol. 2015 Aug;155:49-57. doi: 10.1016/j.exppara.2015.05.006. Epub 2015 May 14.


A subclass of eukaryotic proteins is subject to modification with fatty acids, the most common of which are palmitic and myristic acid. Protein acylation allows association with cellular membranes in the absence of transmembrane domains. Here we examine POMP39, a protein previously described to be present in the outer mitochondrial membrane proteome (POMP) of the protozoan parasite Trypanosoma brucei. POMP39 lacks canonical transmembrane domains, but is likely both myristoylated and palmitoylated on its N-terminus. Interestingly, the protein is also dually localized on the surface of the mitochondrion as well as in the flagellum of both insect-stage and the bloodstream form of the parasites. Upon abolishing of global protein acylation or mutation of the myristoylation site, POMP39 relocates to the cytosol. RNAi-mediated ablation of the protein neither causes a growth phenotype in insect-stage nor bloodstream form trypanosomes.

Keywords: African trypanosomes; Dual localization of proteins; Mitochondrial outer membrane proteome; Myristoylation/palmitoylation; Protein acylation; Protein targeting.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acylation
  • Animals
  • Cell Line
  • Computational Biology
  • Fatty Acids / analysis*
  • Flagella / chemistry
  • Mice
  • Mitochondria / chemistry*
  • Myristic Acid / metabolism
  • Open Reading Frames
  • Palmitic Acid / metabolism
  • Proteome / chemistry*
  • Proteome / genetics
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / genetics
  • Rabbits
  • Trypanosoma brucei brucei / chemistry*
  • Trypanosoma brucei brucei / genetics
  • Trypanosoma brucei brucei / ultrastructure


  • Fatty Acids
  • Proteome
  • Protozoan Proteins
  • Myristic Acid
  • Palmitic Acid