Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale

Publication date: 27 June 2017
Source:Cell Reports, Volume 19, Issue 13
Author(s): Marcel Morgenstern, Sebastian B. Stiller, Philipp Lübbert, Christian D. Peikert, Stefan Dannenmaier, Friedel Drepper, Uri Weill, Philipp Höß, Reinhild Feuerstein, Michael Gebert, Maria Bohnert, Martin van der Laan, Maya Schuldiner, Conny Schütze, Silke Oeljeklaus, Nikolaus Pfanner, Nils Wiedemann, Bettina Warscheid
Mitochondria perform central functions in cellular bioenergetics, metabolism, and signaling, and their dysfunction has been linked to numerous diseases. The available studies cover only part of the mitochondrial proteome, and a separation of core mitochondrial proteins from associated fractions has not been achieved. We developed an integrative experimental approach to define the proteome of east mitochondria. We classified > 3,300 proteins of mitochondria and mitochondria-associated fractions and defined 901 high-confidence mitochondrial proteins, expanding the set of mitochondrial proteins by 82. Our analysis includes protein abundance under fermentable and nonfermentable growth, submitochondrial localization, single-protein experiments, and subcellular classification of mitochondria-associated fractions. We identified mitochondrial interactors of respiratory chain supercomplexes, ATP synthase, AAA proteases, the mitochondrial contact site and cristae organizing system (MICOS), and the coenzyme Q biosynthesis cluster, as well as mitochondrial proteins with dual cellular localization. The integrative proteome provides a high-confidence source for the characterization of physiological and pathophysiological functions of mitochondria and their integration into the cellular environment.

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Teaser

Morgenstern et al. describe an integrative organelle proteomics analysis to define the mitochondrial proteome in baker's yeast. The study provides a quantitative footprint of the proteome and its dynamics under different conditions. The results expand the set of proteins assigned to the mitochondria and provide a resource for future mitochondrial research.


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