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

Albisetti, Anna; Wiese, Sebastian; Schneider, André; Niemann, Moritz (2015). A component of the mitochondrial outer membrane proteome of T. brucei probably contains covalent bound fatty acids. Experimental parasitology, 155, pp. 49-57. Elsevier 10.1016/j.exppara.2015.05.006

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Schneider, André and Niemann, Moritz

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

0014-4894

Publisher:

Elsevier

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

10 Jun 2015 13:52

Last Modified:

09 Sep 2017 19:20

Publisher DOI:

10.1016/j.exppara.2015.05.006

BORIS DOI:

10.7892/boris.69275

URI:

https://boris.unibe.ch/id/eprint/69275

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