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dc.contributor.authorWeeks, Mark E
dc.contributor.authorSinclair, John
dc.contributor.authorButt, Amna
dc.contributor.authorChung, Yuen-Li
dc.contributor.authorWorthington, Jessica L
dc.contributor.authorWilkinson, Caroline R M
dc.contributor.authorGriffiths, John R
dc.contributor.authorJones, Nic
dc.contributor.authorWaterfield, Michael D
dc.contributor.authorTimms, John F
dc.date.accessioned2009-07-07T09:58:23Z
dc.date.available2009-07-07T09:58:23Z
dc.date.issued2006-05
dc.identifier.citationA parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe. 2006, 6 (9):2772-96 Proteomicsen
dc.identifier.issn1615-9853
dc.identifier.pmid16548067
dc.identifier.doi10.1002/pmic.200500741
dc.identifier.urihttp://hdl.handle.net/10541/72676
dc.description.abstractUsing an integrated approach incorporating proteomics, metabolomics and published mRNA data, we have investigated the effects of hydrogen peroxide on wild type and a Sty1p-deletion mutant of the fission yeast Schizosaccharomyces pombe. Differential protein expression analysis based on the modification of proteins with matched fluorescent labelling reagents (2-D-DIGE) is the foundation of the quantitative proteomics approach. This study identifies 260 differentially expressed protein isoforms from 2-D-DIGE gels using MALDI MS and reveals the complexity of the cellular response to oxidative stress and the dependency on the Sty1p stress-activated protein kinase. We show the relationship between these protein changes and mRNA expression levels identified in a parallel whole genome study, and discuss the regulatory mechanisms involved in protecting cells against hydrogen peroxide and the involvement of Sty1p-dependent stress-activated protein kinase signalling. Metabolomic profiling of 29 intermediates using 1H NMR was also conducted alongside the protein analysis using the same sample sets, allowing examination of how the protein changes might affect the metabolic pathways and biological processes involved in the oxidative stress response. This combined analysis identifies a number of interlinked metabolic pathways that exhibit stress- and Sty1-dependent patterns of regulation.
dc.language.isoenen
dc.subject.meshElectrophoresis, Gel, Two-Dimensional
dc.subject.meshGene Deletion
dc.subject.meshGene Expression Regulation
dc.subject.meshHydrogen Peroxide
dc.subject.meshMass Spectrometry
dc.subject.meshMitogen-Activated Protein Kinase Kinases
dc.subject.meshMitogen-Activated Protein Kinases
dc.subject.meshOxidants
dc.subject.meshOxidative Stress
dc.subject.meshProtein Isoforms
dc.subject.meshProtein Processing, Post-Translational
dc.subject.meshProteomics
dc.subject.meshRNA, Messenger
dc.subject.meshSchizosaccharomyces
dc.subject.meshSchizosaccharomyces pombe Proteins
dc.titleA parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe.en
dc.typeArticleen
dc.contributor.departmentLudwig Institute for Cancer Research, University College London, Cruciform Building, London, UK.en
dc.identifier.journalProteomicsen
html.description.abstractUsing an integrated approach incorporating proteomics, metabolomics and published mRNA data, we have investigated the effects of hydrogen peroxide on wild type and a Sty1p-deletion mutant of the fission yeast Schizosaccharomyces pombe. Differential protein expression analysis based on the modification of proteins with matched fluorescent labelling reagents (2-D-DIGE) is the foundation of the quantitative proteomics approach. This study identifies 260 differentially expressed protein isoforms from 2-D-DIGE gels using MALDI MS and reveals the complexity of the cellular response to oxidative stress and the dependency on the Sty1p stress-activated protein kinase. We show the relationship between these protein changes and mRNA expression levels identified in a parallel whole genome study, and discuss the regulatory mechanisms involved in protecting cells against hydrogen peroxide and the involvement of Sty1p-dependent stress-activated protein kinase signalling. Metabolomic profiling of 29 intermediates using 1H NMR was also conducted alongside the protein analysis using the same sample sets, allowing examination of how the protein changes might affect the metabolic pathways and biological processes involved in the oxidative stress response. This combined analysis identifies a number of interlinked metabolic pathways that exhibit stress- and Sty1-dependent patterns of regulation.


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