Proteomic Analysis of Tardigrades Towards a Better Understanding of Molecular Mechanisms by Anhydrobiotic Organisms 英文参考文献.docVIP

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Proteomic Analysis of Tardigrades Towards a Better Understanding of Molecular Mechanisms by Anhydrobiotic Organisms 英文参考文献.doc

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Proteomic Analysis of Tardigrades Towards a Better Understanding of Molecular Mechanisms by Anhydrobiotic Organisms 英文参考文献

ProteomicAnalysisofTardigrades:TowardsaBetter UnderstandingofMolecularMechanismsby AnhydrobioticOrganisms ElhamSchokraie1,AgnesHotz-Wagenblatt1,UweWarnken1,BrahimMali2,MarcusFrohme2 ,Frank Fo¨rster3,ThomasDandekar3,SteffenHengherr4,RalphO.Schill4,MartinaSchno¨lzer1* 1Functional Proteome Analysis, German Cancer Research Center, Heidelberg, Germany, 2Department of Molecular Biology and Functional Genomics, University of Applied Sciences Wildau, Wildau, Germany, 3Department of Bioinformatics, University of Wu¨rzburg, Wu¨rzburg, Germany, 4Department of Zoology, University of Stuttgart,Stuttgart,Germany Abstract Background: Tardigrades are small, multicellular invertebrates which are able to survive times of unfavourable environmental conditions using their well-known capability to undergo cryptobiosis at any stage of their life cycle. Milnesium tardigradum has become a powerful model system for the analysis of cryptobiosis. While some genetic informationisalreadyavailableforMilnesiumtardigradumtheproteomeisstilltobediscovered. PrincipalFindings:HerewepresenttothebestofourknowledgethefirstcomprehensivestudyofMilnesiumtardigradum ontheproteinlevel.Toestablishaproteomereferencemapwedevelopedoptimizedprotocolsforproteinextractionfrom tardigradesintheactivestateandforseparationofproteinsbyhighresolutiontwo-dimensionalgelelectrophoresis.Since onlylimitedsequenceinformationofM.tardigradumonthegenomeandgeneexpressionlevelisavailabletodateinpublic databases we initiated in parallel a tardigrade EST sequencing project to allow for protein identification by electrospray ionizationtandemmassspectrometry.271outof606analyzedproteinspotscouldbeidentifiedbysearchingagainstthe publicly available NCBInr database as well as our newly established tardigrade protein database corresponding to 144 uniqueproteins.Another150spotscouldbeidentifiedinthetardigradeclusteredESTdatabasecorrespondingto36unique contigs and ESTs. Proteins with annotated function were further categorized in more detai