N-Terminal Domain of Nuclear IL-1α Shows Structural Similarity to the C-Terminal Domain of Snf1 and Binds to the HATCore Module of the SAGA Complex 英文参考文献.docVIP

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N-Terminal Domain of Nuclear IL-1α Shows Structural Similarity to the C-Terminal Domain of Snf1 and Binds to the HATCore Module of the SAGA Complex 英文参考文献.doc

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N-Terminal Domain of Nuclear IL-1α Shows Structural Similarity to the C-Terminal Domain of Snf1 and Binds to the HATCore Module of the SAGA Complex 英文参考文献

N-TerminalDomainofNuclearIL-1aShowsStructural SimilaritytotheC-TerminalDomainofSnf1andBindsto theHAT/CoreModuleoftheSAGAComplex BlankaZamostna1,JosefNovak1,VaclavVopalensky1,TomasMasek1,LadislavBurysek2, MartinPospisek1* 1DepartmentofGeneticsandMicrobiology,FacultyofScience,CharlesUniversityinPrague,Prague,CzechRepublic,2Proteans.r.o.,DobraVodauCeskychBudejovic, CzechRepublic Abstract Interleukin-1a(IL-1a)isaproinflammatorycytokineandakeyplayerinhostimmuneresponsesinhighereukaryotes.IL-1a has pleiotropic effects on a wide range of cell types, and it has been extensively studied for its ability to contribute to various autoimmune and inflammation-linked disorders, including rheumatoid arthritis, Alzheimer’s disease, systemic sclerosisandcardiovasculardisorders.Interestingly,asignificantproportionofIL-1aistranslocatedtothecellnucleus,in whichitinteractswithhistoneacetyltransferasecomplexes.DespitetheimportanceofIL-1a,littleisknownregardingits bindingtargetsandfunctionsinthenucleus.Wetookadvantageofthehistoneacetyltransferase(HAT)complexesbeing evolutionarilyconservedfromyeasttohumansandtheyeastSAGAcomplexservingasanepitomeoftheeukaryoticHAT complexes.Usinggeneknock-outtechniqueandco-immunoprecipitationoftheIL-1aprecursorwithTAP-taggedsubunits oftheyeastHATcomplexes,wemappedtheIL-1a-bindingsitetotheHAT/CoremoduleoftheSAGAcomplex.Wealso predicted the 3-D structure of the IL-1a N-terminal domain, and by employing structure similarity searches, we found asimilarstructureintheC-terminalregulatoryregionofthecatalyticsubunitoftheAMP-activated/Snf1proteinkinases, which interact withHAT complexes both in mammals andyeast, respectively. This finding is further supported with the abilityoftheIL-1aprecursortopartiallyrescuegrowthdefectsofsnf1Dyeaststrainsonmediacontaining3-Amino-1,2,4- triazole(3-AT),acompetitiveinhibitorofHis3.Finally,thecarefulevaluationofourdatatogetherwithotherpublisheddata inthefieldallowsustohypothesizeanewfunctionfortheADAcomplexinSAGAcomplexassembly. Ci