What can a unicellular parasite tell us about mitochondrial biogenesis?

Most of what we know about mitochondrial biogenesis stems from work in yeast and mammals, which are quite closely related. To understand the conserved features of mitochondria and the evolutionary forces that shaped it, it is important to study a more diverse group of eukaryotes. The parasitic protozoan Trypanosoma brucei and its relatives are excellent systems to do so, since they appear to have diverged from other eukaryotes very early in evolution. This is reflected in a number of unique and extreme features in their mitochondrial biology, including a single continuous mitochondrion that contains a one unit mitochondrial genome that is physically connected across the two membranes with the basal body of the flagellum. Moreover, many mitochondrial transcripts have to be extensively edited in order to become functional mRNAs and organellar translation requires extensive import of cytosolic tRNAs. In my talk I will focus on the discovery and characterization of the elusive mitochondrial protein import system of the mitochondrial outer membrane of trypanosomes. In addition I will present data on a central outer membrane component of the mitochondrial genome inheritance system of T. brucei and compare it to the better characterized system of yeast. - I hope that I can convince you in my talk, that a better understanding of the mitochondrial biology in T. brucei will provide insights into both fundamentally conserved and fundamentally diverged aspects of mitochondrial biogenesis and thus of the evolutionary history of mitochondria in general.

Zendšraiben an maine gloibens-genossen in Hamburg oder eine abhandlung iber den iśraeliṭišen kulṭus

[Lazarus Jakob Riesser]

Sēfer Yōsîppôn : di bšreibung aler merkwirdign begebnheiṭen fon anfang der welṭ... biz Ṭiṭus hoṭ ... dos heilige hoiz dos Bes-hamikdeš ferbrenṭ...

[Yôsēf Ben-Gōryôn hak-kōhēn]

Sēfer Kōkevā de-šāvît : hû hak-kôkāv ašer ʿāvar ... hay-yir'at šāmayim le-nāšîm ... li-lešôn aškenaz û-niqrā šemô <šṭerin šus>

Digitalisat der Ausg. Amśṭrdm, 1694/95

Forṭunaṭus miṭ zain sekl un winšhiṭlein : wi er dozelbigi bikumn un im domiṭ ergangn ; in einr ibroiz luśịgn lebnś bešraibung for gišṭelṭ un itzund tzum erśṭn mol alzo gidrukṭ

Digitalisat der Ausg. [Frankfurt am Main], [1699]

Great expectations: what can fMRI research tell us about psychological phenomena?

Expectations for what functional magnetic resonance imaging (fMRI) can offer psychophysiology vary greatly. Overreaching enthusiasm such as the idea that fMRI can reveal lies and political attitudes are as common as the opinion that fMRI, in its current form, is useless for the advancement of psychological theories. Errors in the inferences being drawn from fMRI data may be contributing to each of these extreme positions, so the present paper addresses these several common inferential errors and describes some of the potential of fMRI for psychophysiological theory and research.

What can a unicellular parasite tell us about mitochondrial biogenesis?

In the unicellular parasite Trypanosoma brucei, as in other eukaryotes, more than 95% of all mitochondrial proteins are imported from the cytosol. The recently characterized multisubunit ATOM complex, the functional analogue of the TOM complex of yeast, mediates import of essentially all proteins across the outer mitochondrial membrane in T. brucei. Moreover, an additional protein termed pATOM36, which is loosely associated with the ATOM complex, has been implicated in the import of only a subset of mitochondrial proteins. Here we have investigated more precisely which role pATOM36 plays in mitochondrial protein import. RNAi mediated ablation of pATOM36 specifically depletes a subset of outer mitochondrial membrane proteins including ATOM complex subunits and as a consequence results in the collapse of the ATOM complex as shown by Blue native PAGE. In addition, a SILAC-based global proteomic analysis of uninduced and induced pATOM36 RNAi cells together with in vitro import experiments suggest that pATOM36 might be a novel protein import factor acting on a subset of alpha-helically anchored mitochondrial outer membrane proteins. Identification of pATOM36 interaction partners by co-immunoprecipitation together with immunofluorescence analysis shows that unexpectedly a fraction of the protein is associated with the tripartite attachment complex (TAC). This complex is essential for proper inheritance of the mitochondrial DNA in T. brucei. It forms a physical connection between the single unit mitochondrial DNA and the basal body of the flagellum that is stable throughout the cell cycle. Thus, pATOM36 simultaneously mediates ATOM assembly, and thus protein import, as well as mitochondrial DNA inheritance since it is an essential component of the TAC.