Characterization, design, and function of the mitochondrial proteome: from organs to organisms
| Autor: | Jeong H. Choi, David A. Liem, Tao Xu, Caitlin M. Black, Yueju Wang, Peipei Ping, John R. Yates, Henning Hermjakob, Ning Deng, Amanda J. Lin, Jun Zhang, Nobel C. Zong, James N. Weiss, Christopher Lotz, Rolf Apweiler, Edward Lau, Paavo Korge |
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| Rok vydání: | 2014 |
| Předmět: |
Electrophoresis
Biochemistry & Molecular Biology Proteome 1.1 Normal biological development and functioning Computational biology Mitochondrion intergenomic Bioinformatics Biochemistry Genome Article proteomic comparisons Mitochondrial Proteins Mice mitochondrial function Tandem Mass Spectrometry Underpinning research Genetics Animals Humans mitochondrial proteome Gene Chromatography Liquid Polyacrylamide Gel heart diseases biology General Chemistry Biological Sciences biology.organism_classification Phenotype Mitochondrial proteome Drosophila melanogaster Chemical Sciences intragenomic Electrophoresis Polyacrylamide Gel Generic health relevance Energy source Chromatography Liquid Biotechnology |
| Zdroj: | Journal of proteome research, vol 13, iss 2 |
| Popis: | Mitochondria are a common energy source for organs and organisms; their diverse functions are specialized according to the unique phenotypes of their hosting environment. Perturbation of mitochondrial homeostasis accompanies significant pathological phenotypes. However, the connections between mitochondrial proteome properties and function remain to be experimentally established on a systematic level. This uncertainty impedes the contextualization and translation of proteomic data to the molecular derivations of mitochondrial diseases. We present a collection of mitochondrial features and functions from four model systems, including two cardiac mitochondrial proteomes from distinct genomes (human and mouse), two unique organ mitochondrial proteomes from identical genetic codons (mouse heart and mouse liver), as well as a relevant metazoan out-group (drosophila). The data, composed of mitochondrial protein abundance and their biochemical activities, capture the core functionalities of these mitochondria. This investigation allowed us to redefine the core mitochondrial proteome from organs and organisms, as well as the relevant contributions from genetic information and hosting milieu. Our study has identified significant enrichment of disease-associated genes and their products. Furthermore, correlational analyses suggest that mitochondrial proteome design is primarily driven by cellular environment. Taken together, these results connect proteome feature with mitochondrial function, providing a prospective resource for mitochondrial pathophysiology and developing novel therapeutic targets in medicine. |
| Databáze: | OpenAIRE |
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