Origin and Evolution of Retinoid Isomerization Machinery in Vertebrate Visual Cycle Hint from Jawless Vertebrates 英文参考文献.docVIP

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Origin and Evolution of Retinoid Isomerization Machinery in Vertebrate Visual Cycle Hint from Jawless Vertebrates 英文参考文献.doc

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Origin and Evolution of Retinoid Isomerization Machinery in Vertebrate Visual Cycle Hint from Jawless Vertebrates 英文参考文献

OriginandEvolutionofRetinoidIsomerization MachineryinVertebrateVisualCycle:HintfromJawless Vertebrates EugeniaPoliakov1.,AlexanderN.Gubin1.,OliviaStearn1,YanLi1,MariaMercedesCampos2, SusanGentleman1,IgorB.Rogozin3,T.MichaelRedmond1* 1LaboratoryofRetinalCellMolecularBiology,NationalEyeInstitute,NationalInstitutesofHealth,Bethesda,Maryland,UnitedStatesofAmerica,2BiologicalImaging Core,NationalEyeInstitute,NationalInstitutesofHealth,Bethesda,Maryland,UnitedStatesofAmerica,3NationalCenterforBiotechnologyInformation,NationalLibrary ofMedicine,NationalInstitutesofHealth,Bethesda,Maryland,UnitedStatesofAmerica Abstract Inordertomaintainvisualsensitivityatalllightlevels,thevertebrateeyepossessesamechanismtoregeneratethevisual pigmentchromophore11-cisretinalinthedarkenzymatically,unlikeinallothertaxa,whichrelyonphotoisomerization. Thismechanismistermedthevisualcycleandislocalizedtotheretinalpigmentepithelium(RPE),asupportlayerofthe neural retina. Speculation has long revolved around whether more primitive chordates, such as tunicates and cephalochordates, anticipated this feature. The two key enzymes of the visual cycle are RPE65, the visual cycle all-trans retinyl ester isomerohydrolase, and lecithin:retinol acyltransferase (LRAT), which generates RPE65’s substrate. We hypothesized that the origin of the vertebrate visual cycle is directly connected to an ancestral carotenoid oxygenase acquiring a new retinyl ester isomerohydrolase function. Our phylogenetic analyses of the RPE65/BCMO and N1pC/P60 (LRAT) superfamilies show that neither RPE65 nor LRAT orthologs occur in tunicates (Ciona) or cephalochordates (Branchiostoma),butoccurinPetromyzonmarinus(SeaLamprey),ajawlessvertebrate.TheclosesthomologstoRPE65in CionaandBranchiostomalackedpredictedfunctionallydivergedresiduesfoundinallauthenticRPE65s,butlampreyRPE65 contained all of them. We cloned RPE65 and LRATb cDNAs from lamprey RPE and demonstrated appropriate enzymatic activities.WeshowthatCiona?-carotenemonooxygenas