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1、72aSunday,February8,2015regionandsoallowsthehelicaseandpolymerasetobindandbeginunwinding366-PosBoardB146andreplication,respecively.AftertravellingallaroundtheplasmidprobablyasTheEffectofSingle-StrandedDNABindingProteinRPA2onXPDasingleproteincomplex,theproteinsthenreachthenewlys
2、ynthesisedoriginHelicaseProcessivityofreplication,whichprovidesthesignalfortermination.RepDthendoesaBarbaraStekas1,ZhiQi2,MasayoshiHonda3,MariaSpies4,YannChemla1.1seriesofstrandexchangestoclosethetwoplasmidcircles.Physics,UniversityofIllinois-Urbana-Champaign,Urbana,IL,USA,23We
3、areusingacombinationofmeasurementswithwholeplasmidsandoligo-ColumbiaUniversity,NewYork,NY,USA,UniversityofCalifornia,4nucleotidemodelstoelucidatetheseriesofeventsateachstageofthereplica-Davis,Davis,CA,USA,Biochemistry,UniversityofIowa,IowaCity,tion.Inparticular,byfollowingindiv
4、idualprocessesinrealtime,weareabletoIA,USA.describetheorderofbiochemicalstepsthatenablethisprocesstooccur.FacXPDhelicaseisthearchaealhomologofyeastRad3andhumanxerodermapigmentosumgroupDprotein(XPD)fromtheorganismFerroplasmaacidarma-363-PosBoardB143nus.Thisenzymeservesasamodelfo
5、runderstandingthemolecularmechanismCooperativeActivityofSARSCoronavirusNsp13HelicaseCharacterizedofhumansuperfamily2BhelicaseXPDinvolvedintranscriptioninitiationandbySingleMoleculeFRETnucleotideexcisionrepair.PreviousworkhasshownthattheunwindingofHyeryeonIm,SangmiJee,GwangrogLe
6、e.double-strandedDNAbyFacXPDisregulatedbythesingle-strandedDNALifeScience,GwangjuInstituteofScienceandTechnology,Gwangju,bindingproteinFacRPA2.However,themechanismbywhichthisoccursisun-Korea,Republicof.known.Here,wepresentasinglemoleculestudyofthisregulationusingopticalSARSwase
7、pidemicin2003worldwide.SARS-CoVhelicaseplayscriticaltraps.WeshowthatXPDisaweakhelicaseasamonomer,onlyabletounwindrolesinviralreplication,andhasbeenproposedtobeapotentialcandidateshortdistances(~12bp)undertensionappliedbytheopticaltraps,withastrongforanti-SARStherapy.Weusesingle
8、moleculefluorescenceresonanceenergydependenceonDNAseque
