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MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data

Mitochondria are a vital component of eukaryotic cells with functions that extend beyond energy production to include metabolism, signaling, cell growth, and apoptosis. Their dysfunction is implicated in a large number of metabolic, degenerative, and age-related human diseases. Therefore, it is impo...

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Detalles Bibliográficos
Autores principales: Smith, Anthony C., Robinson, Alan J.
Formato: Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2690483/
https://www.ncbi.nlm.nih.gov/pubmed/19208617
http://dx.doi.org/10.1074/mcp.M800373-MCP200
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author Smith, Anthony C.
Robinson, Alan J.
author_facet Smith, Anthony C.
Robinson, Alan J.
author_sort Smith, Anthony C.
collection PubMed
description Mitochondria are a vital component of eukaryotic cells with functions that extend beyond energy production to include metabolism, signaling, cell growth, and apoptosis. Their dysfunction is implicated in a large number of metabolic, degenerative, and age-related human diseases. Therefore, it is important to characterize and understand the mitochondrion. Many experiments have attempted to define the mitochondrial proteome, resulting in large and complex data sets that are difficult to analyze. To address this, we developed a new public resource for the storage and investigation of this mitochondrial proteomics data, called MitoMiner, that uses a model to describe the proteomics data and associated biological information. The proteomics data of 33 publications from both mass spectrometry and green fluorescent protein tagging experiments were imported and integrated with protein annotation from UniProt and genome projects, metabolic pathway data from Kyoto Encyclopedia of Genes and Genomes, homology relationships from HomoloGene, and disease information from Online Mendelian Inheritance in Man. We demonstrate the strengths of MitoMiner by investigating these data sets and show that the number of different mitochondrial proteins that have been reported is about 3700, although the number of proteins common to both animals and yeast is about 1400, and membrane proteins appear to be underrepresented. Furthermore analysis indicated that enzymes of some cytosolic metabolic pathways are regularly detected in mitochondrial proteomics experiments, suggesting that they are associated with the outside of the outer mitochondrial membrane. The data and advanced capabilities of MitoMiner provide a framework for further mitochondrial analysis and future systems level modeling of mitochondrial physiology.
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spelling pubmed-26904832009-07-24 MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data Smith, Anthony C. Robinson, Alan J. Mol Cell Proteomics Research Mitochondria are a vital component of eukaryotic cells with functions that extend beyond energy production to include metabolism, signaling, cell growth, and apoptosis. Their dysfunction is implicated in a large number of metabolic, degenerative, and age-related human diseases. Therefore, it is important to characterize and understand the mitochondrion. Many experiments have attempted to define the mitochondrial proteome, resulting in large and complex data sets that are difficult to analyze. To address this, we developed a new public resource for the storage and investigation of this mitochondrial proteomics data, called MitoMiner, that uses a model to describe the proteomics data and associated biological information. The proteomics data of 33 publications from both mass spectrometry and green fluorescent protein tagging experiments were imported and integrated with protein annotation from UniProt and genome projects, metabolic pathway data from Kyoto Encyclopedia of Genes and Genomes, homology relationships from HomoloGene, and disease information from Online Mendelian Inheritance in Man. We demonstrate the strengths of MitoMiner by investigating these data sets and show that the number of different mitochondrial proteins that have been reported is about 3700, although the number of proteins common to both animals and yeast is about 1400, and membrane proteins appear to be underrepresented. Furthermore analysis indicated that enzymes of some cytosolic metabolic pathways are regularly detected in mitochondrial proteomics experiments, suggesting that they are associated with the outside of the outer mitochondrial membrane. The data and advanced capabilities of MitoMiner provide a framework for further mitochondrial analysis and future systems level modeling of mitochondrial physiology. American Society for Biochemistry and Molecular Biology 2009-06 /pmc/articles/PMC2690483/ /pubmed/19208617 http://dx.doi.org/10.1074/mcp.M800373-MCP200 Text en Copyright © 2009, The American Society for Biochemistry and Molecular Biology Author's Choice - Final Version Full Access NIH Funded Research - Final Version Full Access Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles
spellingShingle Research
Smith, Anthony C.
Robinson, Alan J.
MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data
title MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data
title_full MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data
title_fullStr MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data
title_full_unstemmed MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data
title_short MitoMiner, an Integrated Database for the Storage and Analysis of Mitochondrial Proteomics Data
title_sort mitominer, an integrated database for the storage and analysis of mitochondrial proteomics data
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2690483/
https://www.ncbi.nlm.nih.gov/pubmed/19208617
http://dx.doi.org/10.1074/mcp.M800373-MCP200
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