Double Domain Swapping in Bovine Seminal RNase Formation of Distinct N- and C-swapped Tetramers and Multimers with Increasing Biological Activities 英文参考文献.docVIP

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Double Domain Swapping in Bovine Seminal RNase Formation of Distinct N- and C-swapped Tetramers and Multimers with Increasing Biological Activities 英文参考文献.doc

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Double Domain Swapping in Bovine Seminal RNase Formation of Distinct N- and C-swapped Tetramers and Multimers with Increasing Biological Activities 英文参考文献

DoubleDomainSwappinginBovineSeminalRNase: FormationofDistinctN-andC-swappedTetramersand MultimerswithIncreasingBiologicalActivities GiovanniGotte1*,AlexanderMahmoudHelmy1,CarmineErcole2,RobertaSpadaccini3, DouglasV.Laurents4,MassimoDonadelli1,DeliaPicone2 1DipartimentodiScienzedellaVitaedellaRiproduzione,SezionediChimicaBiologica,Universita`degliStudidiVerona,Verona,Italy,2DipartimentodiScienzeChimiche, Universita` degli Studi di Napoli ‘‘Federico II’’, Naples, Italy, 3Dipartimento di Scienze Biologiche e Ambientali, Universita` del Sannio, Benevento, Italy, 4Instituto de Qu?′micaF?′sica‘‘Rocasolano’’(C.S.I.C.),Madrid,Spain Abstract Bovineseminal(BS)RNase,theuniquenativelydimericmemberoftheRNasesuper-family,representsaspecialcasenot onlyforitsadditionalbiologicalactionsbutalsoforthesingularfeaturesof3Ddomainswapping.Thenativeenzymeis indeedamixtureoftwoisoforms:M=M,adimerheldtogetherbytwointer-subunit disulfidebonds,andMxM,70% of thetotal,which,besidesthetwomentioneddisulfides,isadditionallystabilizedbytheswappingofitsN-termini. When lyophilized from 40% acetic acid, BS-RNase oligomerizes as the super-family proto-type RNase A does. In this paper, we induced BS-RNase self-association and analyzed the multimers by size-exclusion chromatography, cross-linking, electrophoresis, mutagenesis, dynamic light scattering, molecular modelling. Finally, we evaluated their enzymatic and cytotoxicactivities. SeveralBS-RNasedomain-swappedoligomersweredetected,includingtwotetramers,oneexchanging onlytheN-termini,theotherbeingeitherN-orC-swapped.TheC-swappingevent,confirmedbyresultsonaBS-K113N mutant,hasbeenfirstlyseeninBS-RNasehere,andprobablystabilizesalsomultimerslargerthantetramers. Interestingly, allBS-RNaseoligomersaremoreenzymaticallyactivethanthenativedimerand,aboveall,theydisplayacytotoxicactivity that definitely increases with the molecular weight of the multimers. This latter feature, to date unknown for BS-RNase, suggestsagainthattheself-as