A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe.

2.50
Hdl Handle:
http://hdl.handle.net/10541/72676
Title:
A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe.
Authors:
Weeks, Mark E; Sinclair, John; Butt, Amna; Chung, Yuen-Li; Worthington, Jessica L; Wilkinson, Caroline R M; Griffiths, John R; Jones, Nic; Waterfield, Michael D; Timms, John F
Abstract:
Using 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.
Affiliation:
Ludwig Institute for Cancer Research, University College London, Cruciform Building, London, UK.
Citation:
A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe. 2006, 6 (9):2772-96 Proteomics
Journal:
Proteomics
Issue Date:
May-2006
URI:
http://hdl.handle.net/10541/72676
DOI:
10.1002/pmic.200500741
PubMed ID:
16548067
Type:
Article
Language:
en
ISSN:
1615-9853
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
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.en
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

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