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Characterization of the mitochondrial proteome of human cells (MitoCoP)

ABSTRACT: The overall aim of the project is the definition and characterization of the mitochondrial proteome of human cells, referred to as MitoCoP. To this end, we combined the complementary strengths of subtractive proteomics, ImportOmics and subcellular protein profiling in a global multidimensional classification approach (see dataset PXD016924). In this part of the project, we (1) performed subtractive proteomics experiments of gradient-purified versus crude mitochondrial fractions prepared from multiple cell lines (multi-cell lines pM-vs-cM experiments), (2) studied the organization of mitochondrial proteins in large functional assemblies by Blue Native (BN) complexome profiling, and (3) analyzed the effect of LYRM9 knockout on mitochondrial protein complexes by BN-PAGE (LYRM9KO-vs-control experiment) to complement the characterization of MitoCoP.

INSTRUMENT(S): LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Friedel Drepper

LAB HEAD: Prof. Dr. Bettina Warscheid

PROVIDER: PXD028149 | Pride | 2021-11-25

REPOSITORIES: Pride

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	ELITE-RSLC022735.raw	Raw
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Definition and characterization of the mitochondrial proteome of human cells (MitoCoP)

Project description:Aim of this project was the definition and characterization of the mitochondrial proteome of human cells, referred to as MitoCoP. To this end, we combined the complementary strengths of subtractive proteomics, ImportOmics and subcellular protein profiling in a global multidimensional classification approach. This multifaceted human mitochondria-centered analysis was expanded to a functional characterization of the mitochondrial proteome. The association of proteins with mitochondrial membranes was assessed by quantitative proteomic and single-protein studies. Protein copy numbers per mitochondrial unit were determined followed by a thorough compilation and functional classification of a high-quality human mitochondrial proteome. We further examined the organization of mitochondrial proteins in large functional assemblies by Blue Native (BN) complexome profiling and characterized functional protein networks of so far not described mitochondrial constituents by quantitative affinity purification mass spectrometry (q-AP-MS) and biochemical analysis. And finally, we systematically studied mitochondrial proteome dynamics and established a comprehensive subunit-resolved turnover map of large membrane protein machineries and central biosynthesis pathways of human mitochondria.

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