The proteome of Saccharomyces cerevisiae mitochondria

TLDR

A quarter of the identified mitochondrial proteins have unknown functions. The study aimed to comprehensively determine the Saccharomyces cerevisiae mitochondrial proteome to serve as a database for exploring mitochondrial functions and diseases. Highly pure mitochondria were fractionated by multiple methods and analyzed by tandem mass spectrometry to identify proteins. The analysis identified 750 proteins, covering ~90 % of the mitochondrial proteome, including all known components of oxidative phosphorylation, the TCA cycle, and mitochondria‑encoded proteins, indicating extensive involvement in cellular processes.

Abstract

We performed a comprehensive approach to determine the proteome of Saccharomyces cerevisiae mitochondria. The proteins of highly pure yeast mitochondria were separated by several independent methods and analyzed by tandem MS. From >20 million MS spectra, 750 different proteins were identified, indicating an involvement of mitochondria in numerous cellular processes. All known components of the oxidative phosphorylation machinery, the tricarboxylic acid cycle, and the stable mitochondria-encoded proteins were found. Based on the mitochondrial proteins described in the literature so far, we calculate that the identified proteins represent ≈90% of all mitochondrial proteins. The function of a quarter of the identified proteins is unknown. The mitochondrial proteome will provide an important database for the analysis of new mitochondrial and mitochondria-associated functions and the characterization of mitochondrial diseases.