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1、ResearchLysineAcetylationIsaHighlyAbundantandEvolutionarilyConservedModificationinEscherichiaColi*□SJunmeiZhang‡§,RobertSprung‡§¶,JiminPei‡,XiaohongTan**,SungchanKim‡‡,HengZhu§§,Chuan-FaLiu**,NickV.Grishin‡,andYingmingZhao‡¶¶LysineacetylationanditsregulatoryenzymesareknownEmergingevidencesugg
2、estsdiversenon-nuclearrolesoftohavepivotalrolesinmammaliancellularphysiology.lysineacetylationanditsregulatoryenzymes,inadditiontoitsHowever,theextentandfunctionofthismodificationinwellrecognizedfunctionsinDNA-templatedprocesses.Forprokaryoticcellsremainlargelyunexplored,therebypre-example,Sirt
3、1modulatesdiversecellularprocesses,suchassentingahurdletofurtherfunctionalstudyofthismodi-fatmetabolism,insulinproduction,glucosehomeostasis,andficationinprokaryoticsystems.Herewereportthefirstcellsurvival,ofwhichsomearemediatedthroughnon-nuclearglobalscreeningoflysineacetylation,identifying138
4、proteins(6–8).Threemembersofthesirtuinfamily(Sirt3,modificationsitesin91proteinsfromEscherichiacoli.NoneoftheproteinshasbeenpreviouslyassociatedwithSirt4,andSirt5)arelocatedinthemitochondrion(9).Acti-thismodification.Amongtheidentifiedproteinsaretran-vationofSirt1,amammalianorthologofyeastSir2,
5、byscriptionalregulators,aswellasotherswithdiversefunc-resveratrolleadstodiversemetabolicchangesinanimalstions.Interestingly,morethan70%oftheacetylatedpro-(10).Therolesoflysineacetylationinmetabolismarefurtherteinsaremetabolicenzymesandtranslationregulators,exemplifiedbythefactsthatthemodificati
6、onispresentinsuggestinganintimatelinkofthismodificationtoenergymorethan20%ofmitochondrialproteinsandishighlymetabolism.Thenewdatasetsuggeststhatlysineacety-enrichedamongmetabolicenzymes(11–14).Althoughthelationcouldbeabundantinprokaryoticcells.Inaddition,inventoryandbiologicalfunctionsoflysinea
7、cetylationsub-theseresultsalsoimplythatfunctionsoflysineacetyla-stratesineukaryoticcellshavebeguntounfold,especiallytionbeyondregulationofgeneexpressionareevolution-arilyconservedfrombacteriatomammals.Furthermore,inhistoneproteins