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Definition of a high-confidence mitochondrial proteome at quantitative scale_absolute quantification of carbon source-dependent protein expression

ABSTRACT: Mitochondria perform central functions in cellular bioenergetics, metabolism and signaling and their malfunction 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, quantitative MS-based experimental approach to define the high confidence proteome of yeast mitochondria and to identify new mitochondrial proteins. The analysis includes protein abundance under fermentable and non-fermentable growth, submitochondrial localization, single-protein analysis and subcellular classification of mitochondria-associated fractions. We identified novel mitochondrial interactors of respiratory chain supercomplexes, ATP synthase, AAA proteases, the mitochondrial contact site and cristae organizing system (MICOS) and coenzyme Q biosynthesis cluster as well as new 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Christian D. Peikert

LAB HEAD: Prof. Dr. Bettina Warscheid

PROVIDER: PXD006146 | Pride | 2017-06-29

REPOSITORIES: Pride

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Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale.

Morgenstern Marcel M Stiller Sebastian B SB Lübbert Philipp P Peikert Christian D CD Dannenmaier Stefan S Drepper Friedel F Weill Uri U Höß Philipp P Feuerstein Reinhild R Gebert Michael M Bohnert Maria M van der Laan Martin M Schuldiner Maya M Schütze Conny C Oeljeklaus Silke S Pfanner Nikolaus N Wiedemann Nils N Warscheid Bettina B

Cell reports 20170601 13

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 yeast mitochondria. We classified > 3,300 proteins of mitochondria and mitochondria-associated fractions ...[more]

PMID: 28658629

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Project description:Maintenance of the correct level and organization of nucleosomes is crucial for genome function. Here we uncover a role for a conserved bromodomain AAA-ATPase, Abo1, in maintenance of nucleosome architecture in fission yeast. Cells lacking abo1+ experience both a reduction and mis-positioning of nucleosomes at transcribed sequences in addition to increased intragenic transcription, phenotypes that are hallmarks of defective chromatin re-establishment behind RNA polymerase II. Abo1 is recruited to gene sequences and associates with histone H3 and the histone chaperone FACT. Furthermore, the distribution of Abo1 on chromatin is disturbed by impaired FACT function. The role of Abo1 extends to some promoters and also to silent heterochromatin. Abo1 is recruited to pericentromeric heterochromatin independently of the HP1 ortholog, Swi6, where it enforces proper nucleosome occupancy. Consequently, loss of Abo1 alleviates silencing and causes elevated chromosome mis-segregation. We suggest that Abo1 provides a histone chaperone function that maintains nucleosome architecture genome-wide. A chromatin-seq/MNase-seq approach called Chromatin Particle Spectrum Analysis (Kent et al., (2011) Nucleic Acids Res. 39:e26) was used to map and compare nucleosome position in wild-type (strain 972) and isogenic abo1 knock-out (strain HM463) fission yeast cells. For each strain, three independent in vivo MNase digest bio-reps were performed and the purified DNA pooled. CPSA was performed using paired-end mode Illumina technology with pooled samples multiplexed over two HiSeq2000 lanes. Each CPSA paired read describes a microcococcal nuclease (MNase) resistant DNA species from chromatin, with the insert-size equivalent to the size of DNA protection. For each strain type, two analysed data sets are provided here: one listing the genomic distribution of MNase-protected DNAs of 150bp (â150bp CPSA size classâ) and corresponding to mono-nucleosomes; the other listing the genomic distribution of MNase-protected DNAs of 300bp (â300bp CPSA size classâ) and corresponding to di-nucleosomes.

			Action	DRS
	3_Absolutequantification_txt_folder.zip	Other
	QEplus011558.raw	Raw
	QEplus011559.raw	Raw
	QEplus011560.raw	Raw
	QEplus011561.raw	Raw