Biochemical Characterization of a Structure-Specific Resolving Enzyme from Sulfolobus islandicus Rod-Shaped Virus 2 英文参考文献.docVIP

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Biochemical Characterization of a Structure-Specific Resolving Enzyme from Sulfolobus islandicus Rod-Shaped Virus 2 英文参考文献.doc

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Biochemical Characterization of a Structure-Specific Resolving Enzyme from Sulfolobus islandicus Rod-Shaped Virus 2 英文参考文献

BiochemicalCharacterizationofaStructure-Specific ResolvingEnzymefromSulfolobusislandicus Rod-ShapedVirus2 AndrewF.Gardner*,ChudiGuan,WilliamE.Jack NewEnglandBiolabs,Inc.,Ipswich,Massachusetts,UnitedStatesofAmerica Abstract Sulfolobusislandicus rodshapedvirus2(SIRV2)infectsthearchaeonSulfolobus islandicusatextremetemperature (70uC– 80uC)andacidity(pH3).SIRV2encodesaHollidayjunctionresolvingenzyme(SIRV2Hjr)thathasbeenproposedasakey enzyme in SIRV2 genome replication. The molecular mechanism for SIRV2 Hjr four-way junction cleavage bias, minimal requirementsforfour-wayjunctioncleavage,andsubstratespecificityweredetermined.SIRV2Hjrcleavesfour-wayDNA junctionswithapreferenceforcleavageofexchangestrandpairs,incontrasttohost-derivedresolvingenzymes,suggesting fundamentaldifferencesinsubstraterecognitionandcleavageamongcloselyrelatedSulfolobusresolvingenzymes.Unlike other viral resolving enzymes, such as T4 endonuclease VII or T7 endonuclease I, that cleave branched DNA replication intermediates,SIRV2Hjrcleavageisspecifictofour-wayDNAjunctionsandinactiveonotherbranchedDNAmolecules.In addition,aspecificinteractionwasdetectedbetweenSIRV2HjrandtheSIRV2virionbodycoatprotein(SIRV2gp26).Based onthisobservation,amodelisproposedlinkingSIRV2Hjrgenomeresolutiontoviralparticleassembly. Citation:GardnerAF,GuanC,JackWE(2011)BiochemicalCharacterizationofaStructure-SpecificResolvingEnzymefromSulfolobusislandicusRod-ShapedVirus 2.PLoSONE6(8):e23668.doi:10.1371/journal.pone.0023668 Editor:Jean-PierreVartanian,InstitutPasteur,France ReceivedJune2,2011;AcceptedJuly22,2011;PublishedAugust17,2011 Copyright: ? 2011 Gardner 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:ThisworkwassupportedbyNewEnglandBiolabs,Inc().Thefundershadnoroleinstudydesign,datacollectionandanalysis,decision topublish,orpreparati