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TOMM70 ImportOmics analysis of human mitochondria

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 complementary strengths of subtractive proteomics, ImportOmics and subcellular protein profiling in a global multidimensional classification approach (see dataset 'Definition and characterization of the mitochondrial proteome of human cells (MitoCoP)'). TOMM70 ImportOmics experiments were performed to complement the data obtained in TOMM40 ImportOmics experiments.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Friedel Drepper

LAB HEAD: Bettina Warscheid

PROVIDER: PXD018122 | Pride | 2021-11-25

REPOSITORIES: Pride

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	ELITE-RSLC019717.raw	Raw
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Establishment of functional protein interaction networks of so far undescribed human mitochondrial proteins by q-AP-MS

Project description: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 complementary strengths of subtractive proteomics, ImportOmics and subcellular protein profiling in a global multidimensional classification approach (see dataset 'Definition and characterization of the mitochondrial proteome of human cells (MitoCoP)'). SILAC-based affinity purification-mass spectrometry (q-AP-MS) experiments were performed to establish functional protein interaction networks of so far undescribed mitochondrial proteins.

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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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Definition and characterization of the mitochondrial proteome of human cells (MitoCoP): Relation between MS analysis time, sample fractionation, proteases, replicates and number of proteins identified/quantified

Project description:Aim of the overall 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. In this part of the project, we analyzed the correlation between MS analysis time, sample fractionation, use of multiple proteases and replicates on the number of proteins identified and quantified in mitochondrial fractions applying the subtractive proteomics approach.

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Characterization of the mitochondrial proteome of human cells (MitoCoP)

Project description: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.

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Characterization of the mitochondrial proteome of human cells (MitoCoP)

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hnRNP C is a key regulator of protein synthesis in mitosis

Project description:Stringent post-transcriptional regulation of mRNA fate is critical for proper cell division. To detect proteins involved in such regulation, we analyzed the composition of intact polysomal complexes from mitotic and interphase cells by quantitative mass-spectrometry. Using this approach, we detected increased association of several mRNA-binding proteins, including heterogeneous nuclear ribonucleoprotein C (hnRNP C), with mitotic polysomes. Immunofluorescence analysis, puromycin-sensitivity assays and nascent-chain pulldowns confirmed that hnRNP C interacts with polysome-bound mRNA during mitosis. Using a combination of pulsed SILAC and metabolic labeling, we found that knockdown of hnRNP C has a pervasive effect on both global and transcript-specific translation rates. Furthermore, ribosome profiling revealed that hnRNP C is involved in translation of mRNAs encoding components of the translation machinery and other mRNAs harboring a 5' terminal oligopyrimidine tract (5’ TOP). Taken together, these results suggest that hnRNP C is crucial for ribogenesis during mitosis; in its absence, production of ribosomal proteins and translation factors is impaired and translation rates are reduced during subsequent phases of the cell cycle.

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shRNA Sensor Analysis of 5' U converted shRNAs reveals 3' target bias exists in addition to 5' guide bias

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Gene Expression in Castration-Resistant C4-2 Cells after AR Knockdown

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