Prokayrotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium tuberculosis 英文参考文献.docVIP
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Prokayrotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium tuberculosis 英文参考文献
ProkayroticUbiquitin-LikeProtein(Pup)Proteomeof
Mycobacteriumtuberculosis
RichardA.Festa1.,FionaMcAllister2.,MichaelJ.Pearce1.,JulianMintseris2,KristinE.Burns1,StevenP.
Gygi2*,K.HeranDarwin1*
1DepartmentofMicrobiology,NewYorkUniversitySchoolofMedicine,NewYork,NewYork,UnitedStatesofAmerica,2DepartmentofCellBiology,HarvardMedical
School,Boston,Massachusetts,UnitedStatesofAmerica
Abstract
Prokaryotic ubiquitin-like protein (Pup) in Mycobacterium tuberculosis (Mtb) is the first known post-translational small
proteinmodifierinprokaryotes,andtargetsseveralproteinsfordegradationbyabacterialproteasomeinamannerakinto
ubiquitin(Ub)mediatedproteolysisineukaryotes.TodeterminetheextentofpupylationinMtb,weusedtandemaffinity
purification to identify its ‘‘pupylome’’. Mass spectrometry identified 55 out of 604 purified proteins with confirmed
pupylationsites.Forty-fourproteins,includingthosewithandwithoutidentifiedpupylationsites,weretestedassubstrates
ofproteolysisinMtb.Understeadystateconditions,themajorityofthetestproteinsdidnotaccumulateindegradation
mutants, suggesting not all targets of pupylation are necessarily substrates of the proteasome under steady state
conditions.FourproteinsimplicatedinMtbpathogenesis,Icl(isocitratelyase),Ino1(inositol-1-phosphatesynthase),MtrA
(MtbresponseregulatorA)andPhoP(phosphateresponseregulatorP),showedalteredlevelsindegradationdefectiveMtb.
Icl, Ino1andMtrAaccumulatedin Mtbdegradation mutants,suggestingthese proteinsaretargetedtotheproteasome.
Unexpectedly,PhoPwaspresentinwildtypeMtbbutundetectableinthedegradationmutants.Takentogether,thesedata
demonstratethatpupylationregulatesnumerousproteinsinMtbandmaynotalwaysleadtodegradation.
Citation: Festa RA, McAllister F, Pearce MJ, Mintseris J, Burns KE, et al. (2010) Prokayrotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium
tuberculosis.PLoSONE5(1):e8589.doi:10.1371/journal.pone.0008589
Editor:AnilKumarTyagi,UniversityofDelhi,India
ReceivedNovember17,2009;AcceptedDecember9,2009;Publi
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