Promoter Recognition by a Complex of Spx and the C-Terminal Domain of the RNA Polymerase α Subunit 英文参考文献.docVIP

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Promoter Recognition by a Complex of Spx and the C-Terminal Domain of the RNA Polymerase α Subunit 英文参考文献.doc

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Promoter Recognition by a Complex of Spx and the C-Terminal Domain of the RNA Polymerase α Subunit 英文参考文献

Promoter Recognition by a Complex of Spx and the C-Terminal Domain ofthe RNA Polymerase aSubunit MichikoM.Nakano1,AnnLin1,ColeS.Zuber1,KateJ.Newberry2,RichardG.Brennan2,PeterZuber1* 1Department of Science Engineering, School of Medicine, Oregon Health Science University, Beaverton, Oregon, United States of America, 2Department of BiochemistryandMolecularBiology,UniversityofTexas,M.D.AndersonCancerCenter,Texas,UnitedStatesofAmerica Abstract Background:Spx,anArsC(arsenatereductase)familymember,isaglobaltranscriptionalregulatorofthemicrobialstress responseandishighlyconservedamongstGram-positivebacteria.BacillussubtilisSpxproteinexertspositiveandnegative controloftranscriptionthroughitsinteractionwiththeC-terminaldomainoftheRNApolymerase(RNAP)asubunit(aCTD). Spx activates trxA (thioredoxin) and trxB (thioredoxin reductase) in response to thiol stress, and bears an N-terminal C10XXC13redoxdisulfidecenterthatisoxidizedinactiveSpx. Methodology/PrincipalFindings:ThestructureofmutantSpxC10Sshowedachangeintheconformationofhelixa 4.Amino acidsubstitutionsR60EandK62Ewithinandadjacenttohelixa4conferreddefectsinSpx-activatedtranscriptionbutnot Spx-dependent repression. Electrophoretic mobility-shift assays showed aCTD interaction with trxB promoter DNA, but addition of Spx generated a supershifted complex that was disrupted in the presence of reductant (DTT). Interaction of aCTD/SpxcomplexwithpromoterDNArequiredthecis-actingelements-45AGCA-42and-34AGCG-31ofthetrxBpromoter. The SpxG52R mutant, defective in aCTD binding, did not interact with the aCTD-trxB complex. SpxR60E not only failed to complexwithaCTD-trxB,butalsodisruptedaCTD-trxBDNAinteraction. Conclusions/Significance:TheresultsshowthatSpxandaCTDformacomplexthatrecognizesthepromoterDNAofan Spx-controlledgene.AconformationalchangeduringoxidationofSpxtothedisulfideformlikelyaltersthestructureofSpx a helix a4, which contains residues that function in transcriptional activation and aCTD/Spx-promoter interaction. The resul