Polyubiquitin Is Required for Growth, Development and Pathogenicity in the Rice Blast Fungus Magnaporthe oryzae 英文参考文献.docVIP
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Polyubiquitin Is Required for Growth, Development and Pathogenicity in the Rice Blast Fungus Magnaporthe oryzae 英文参考文献
PolyubiquitinIsRequiredforGrowth,Developmentand
PathogenicityintheRiceBlastFungusMagnaporthe
oryzae
YeonyeeOh1,WilliamL.Franck1,Sang-OhHan2,AngelaShows1,EmineGokce3,DavidC.Muddiman3,
RalphA.Dean1*
1CenterforIntegratedFungalResearch,DepartmentofPlantPathology,NorthCarolinaStateUniversity,Raleigh,NorthCarolina,UnitedStatesofAmerica,2Department
ofMedicine,DukeUniversity,Durham, NorthCarolina,UnitedStatesofAmerica, 3W.M.KeckFT-ICRMassSpectrometryLaboratory,DepartmentofChemistry,North
CarolinaStateUniversity,Raleigh,NorthCarolina,UnitedStatesofAmerica
Abstract
Protein ubiquitination, which is highly selective, regulates many important biological processes including cellular
differentiation and pathogenesis in eukaryotic cells. Here, we integrated pharmacological, molecular and proteomic
approaches to explore the role of ubiquitination in Magnaporthe oryzae, the leading fungal disease of rice world-wide.
Inhibition of ubiquitin-mediated proteolysis using the 26S proteasome inhibitor, Bortezomib, significantly attenuated
conidiagermination,appressoriumformationandpathogenicityinM.oryzae.Geneexpressionanalysisrevealedthatmany
genes associated with protein ubiquitination were developmentally regulated during conidia germination. Only a few,
includingapolyubiquitinencodinggene,MGG_01282,weremoreabundantlyexpressedduringappressoriumformation
and under nitrogen starvation. Targeted gene deletion of MGG_01282, in addition to a significant reduction in protein
ubiquitinationasdeterminedbyimmunoblotassays,resultedinpleiotropiceffectsonM.oryzaeincludingreducedgrowth
and sporulation, abnormal conidia morphology, reduced germination and appressorium formation, and the inability to
causedisease.Mutantswerealsodefectiveinsexualdevelopmentandwerefemalesterile.Usingmassspectrometry,we
identified 63 candidate polyubiquitinated proteins under nitrogen starvation, which included overrepresentation of
proteins involved in translation, transport and protein modification. Our study sugges
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