A Protein-Protein Interaction Map of the Trypanosoma brucei Paraflagellar Rod 英文参考文献.docVIP

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A Protein-Protein Interaction Map of the Trypanosoma brucei Paraflagellar Rod 英文参考文献.doc

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A Protein-Protein Interaction Map of the Trypanosoma brucei Paraflagellar Rod 英文参考文献

AProtein-ProteinInteractionMapoftheTrypanosoma bruceiParaflagellarRod SylvainLacomble.,NeilPortman.,KeithGull* SirWilliamDunnSchoolofPathologyandOxfordCentreforIntegrativeSystemsBiology,UniversityofOxford,Oxford,UnitedKingdom Abstract Wehaveconductedaproteininteractionstudyofcomponentswithinaspecificsub-compartmentofaeukaryoticflagellum. The trypanosome flagellum contains a para-crystalline extra-axonemal structure termed the paraflagellar rod (PFR) with aroundfortyidentifiedcomponents.WehaveusedaGatewaycloningapproachcoupledwithyeasttwo-hybrid,RNAiand 2DDiGEtodefineaprotein-proteininteractionnetworktakingplaceinthisstructure.Wedefinetwoclustersofinteractions; thefirstbeingcharacterisedbytwoproteinswithashareddomainwhichisnotsufficientformaintainingtheinteraction. The other cohort is populated by eight proteins, a number of which possess a PFR domain and sub-populations of this network exhibit dependency relationships. Finally, we provide clues as to the structural organisation of the PFR at the molecular level. This multi-strand approach shows that protein interactome data can be generated for insoluble protein complexes. Citation: Lacomble S, Portman N, Gull K (2009) A Protein-Protein Interaction Map of the Trypanosoma brucei Paraflagellar Rod. PLoS ONE 4(11): e7685. doi:10.1371/journal.pone.0007685 Editor:AdamYuan,TemasekLifeSciencesLaboratory,Singapore ReceivedSeptember2,2009;AcceptedOctober12,2009;PublishedNovember3,2009 Copyright: ? 2009 Lacomble et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. Funding: This work was supported by the Wellcome Trust, Human Frontier Science Program, the EP Abraham Trust, the Engineering and Physical Sciences ResearchCouncil(EPSRC)andtheBiotechnologyandBiologicalSciencesResearchCouncil(BBSRC).SLwassupportedbyaHenryGoodgerScholarship.KGisa Wellcome Trus