Evolutionary Dynamics on Protein Bi-stability Landscapes can Potentially Resolve Adaptive Conflicts 英文参考文献.docVIP

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2017-05-11 发布于上海
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Evolutionary Dynamics on Protein Bi-stability Landscapes can Potentially Resolve Adaptive Conflicts 英文参考文献.doc

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Evolutionary Dynamics on Protein Bi-stability Landscapes can Potentially Resolve Adaptive Conflicts 英文参考文献

EvolutionaryDynamicsonProteinBi-stability LandscapesCanPotentiallyResolveAdaptiveConflicts TobiasSikosek1*,ErichBornberg-Bauer1,HueSunChan2 1EvolutionaryBioinformaticsGroup,InstituteforEvolutionandBiodiversity,UniversityofMu¨nster,Mu¨nster,Germany,2DepartmentsofBiochemistry,MolecularGenetics, andPhysics,UniversityofToronto,Toronto,Ontario,Canada Abstract Experimental studies have shown that some proteins exist in two alternative native-state conformations. It has been proposedthatsuchbi-stableproteinscanpotentiallyfunctionasevolutionarybridgesattheinterfacebetweentwoneutral networks of protein sequences that fold uniquely into the two different native conformations. Under adaptive conflict scenarios, bi-stable proteins may be of particular advantage if they simultaneously provide two beneficial biological functions.However,computationalmodelsthatsimulateproteinstructureevolutiondonotyetrecognizetheimportance ofbi-stability.Hereweuseabiophysicalmodeltoanalyzesequencespacetoidentifybi-stableormulti-stableproteinswith two or more equally stable native-state structures. The inclusion of such proteins enhances phenotype connectivity between neutral networks in sequence space. Consideration of the sequence space neighborhood of bridge proteins revealedthatbi-stabilitydecreasesgraduallywitheachmutationthattakesthesequencefurtherawayfromanexactlybi- stableprotein.Withrelaxedselectionpressures,wefoundthatbi-stableproteinsinourmodelarehighlysuccessfulunder simulatedadaptiveconflict.Inspiredbythesemodelpredictions,wedevelopedamethodtoidentifyrealproteinsinthe PDBwithbridge-likeproperties,andhaveverifiedaclearbi-stabilitygradientforaseriesofmutantsstudiedbyAlexanderet al.(ProcNatAcadSciUSA2009,106:21149–21154)thatconnecttwosequencesthatfolduniquelyintotwodifferentnative structures via a bridge-like intermediate mutant sequence. Based on these findings, new testable predictions for future studiesonproteinbi-stabilityandevolutionarediscussed. Citation:SikosekT,Bornberg-BauerE,Cha