A Tethered Bilayer Assembled on Top of Immobilized Calmodulin to Mimic Cellular Compartmentalization 英文参考文献.docVIP

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A Tethered Bilayer Assembled on Top of Immobilized Calmodulin to Mimic Cellular Compartmentalization 英文参考文献.doc

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A Tethered Bilayer Assembled on Top of Immobilized Calmodulin to Mimic Cellular Compartmentalization 英文参考文献

ATetheredBilayerAssembledonTopofImmobilized CalmodulintoMimicCellularCompartmentalization ClaireRossi1,SamahDoumiati1,ClarineLazzarelli2,MarilyneDavi3,FettaMeddar1,DanielLadant3*,Joe¨l Chopineau2,4 * 1UMR 6022 CNRS, Universite′ de Technologie de Compie`gne, Compie`gne, France, 2Universite′ de N??mes, N??mes, France, 3Institut Pasteur, Unite′ de Biochimie des InteractionsMacromole′culaires, CNRSURA2185,Paris,France,4InstitutCharlesGerhardtMontpellier,UMR5253CNRS-ENSCMUM2-UM1EcoleNationaleSupe′rieure de Chimie,Montpellier,France Abstract Background: Biomimetic membrane models tethered on solid supports are important tools for membrane protein biochemistryandbiotechnology.Thesupportedmembranesystemsdescribeduptonowarecomposedofalipidbilayer tetheredornottoasurfaceseparatingtwocompartments:a’’trans’’side,onetoafewnanometerthick,locatedbetween thesupportingsurfaceandthemembrane;anda‘‘cis’’side,abovethesyntheticmembrane,exposedtothebulkmedium. Wedescribehereanovelbiomimeticdesigncomposedofatetheredbilayermembranethatisassembledoverasurface derivatized with a specific intracellular protein marker. This multilayered biomimetic assembly exhibits the fundamental characteristicsofanauthenticbiologicalmembraneincreatingacontinuousyetfluidphospholipidicbarrierbetweentwo distinctcompartments:a‘‘cis’’sidecorrespondingtotheextracellularmilieuanda‘‘trans’’sidemarkedbyakeycytosolic signalingprotein,calmodulin. Methodology/Principal Findings: We established and validated the experimental conditions to construct a multilayered structureconsistinginaplanartetheredbilayerassembledoverasurfacederivatizedwithcalmodulin.Wedemonstrated the following: (i) the grafted calmodulin molecules (in trans side) were fully functional in binding and activating a calmodulin-dependent enzyme, the adenylate cyclase from Bordetella pertussis; and (ii) the assembled bilayer formed a continuous, protein-impermeable boundary that fully separated the underlying calmodulin (trans side) from the above m