Re-Introduction of Transmembrane Serine Residues Reduce the Minimum Pore Diameter of Channelrhodopsin-2 英文参考文献.docVIP

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Re-Introduction of Transmembrane Serine Residues Reduce the Minimum Pore Diameter of Channelrhodopsin-2 英文参考文献.doc

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Re-Introduction of Transmembrane Serine Residues Reduce the Minimum Pore Diameter of Channelrhodopsin-2 英文参考文献

Re-IntroductionofTransmembraneSerineResidues ReducetheMinimumPoreDiameterof Channelrhodopsin-2 RyanRichards,RobertE.Dempski* DepartmentofChemistryandBiochemistry,WorcesterPolytechnicInstitute,Worcester,Massachusetts,UnitedStatesofAmerica Abstract Channelrhodopsin-2 (ChR2) is a microbial-type rhodopsin found in the green algae Chlamydomonas reinhardtii . Under physiologicalconditions,ChR2isaninwardlyrectifyingcationchannelthatpermeatesawiderangeofmono-anddivalent cations. Although this protein shares a high sequence homology with other microbial-type rhodopsins, which are ion pumps,ChR2isanionchannel.AsequencealignmentofChR2withbacteriorhodopsin,aprotonpump,revealsthatChR2 lacksspecificmotifsandresidues,suchasserineandthreonine,knowntocontributetonon-covalentinteractionswithin transmembrane domains. We hypothesized that reintroduction of the eight transmembrane serine residues present in bacteriorhodopsin,butnotinChR2,willrestricttheconformationalflexibilityandreducetheporediameterofChR2.Inthis work, eight single serine mutations were created at homologous positions in ChR2. Additionally, an endogenous transmembrane serine was replaced with alanine. We measured kinetics, changes in reversal potential, and permeability ratiosindifferentalkalimetalsolutionsusingtwo-electrodevoltageclamp.Applyingexcludedvolumetheory,wecalculated theminimumporediameterofChR2constructs.Ananalysisoftheresultsfromourexperimentsshowthatreintroducing serine residues into the transmembrane domain of ChR2 can restrict the minimum pore diameter through inter- and intrahelical hydrogen bonds while the removal of a transmembrane serine results in a larger pore diameter. Therefore, multiplepositionsalongtheintracellularsideofthetransmembranedomainscontributetothecationpermeabilityofChR2. Citation:RichardsR,DempskiRE(2012)Re-IntroductionofTransmembraneSerineResiduesReducetheMinimumPoreDiameterofChannelrhodopsin-2.PLoS ONE7(11):e50018.doi:10.1371/journal.pone.0050018 Editor:Zhong-PingFeng,Universit