title: Chimeric nature of pinopsin between rod and cone visual pigments.
abstract: Chicken pineal pinopsin is the first example of extra-retinal opsins, but little is known about its molecular properties as compared with retinal rod and cone opsins. For characterization of extra-retinal photon signaling, we have developed an overexpression system providing a sufficient amount of purified pinopsin. The recombinant pinopsin, together with similarly prepared chicken rhodopsin and green-sensitive cone pigment, was subjected to photochemical and biochemical analyses by using low-temperature spectroscopy and the transducin activation assay. At liquid nitrogen temperature (-196 degrees C), we detected two kinds of photoproducts, bathopinopsin and isopinopsin, having their absorption maxima (lambda(max)) at 527 and approximately 440 nm, respectively, and we observed complete photoreversibility among pinopsin, bathopinopsin, and isopinopsin. A close parallel of the photoreversibility to the rhodopsin system strongly suggests that light absorbed by pinopsin triggers the initial event of cis-trans isomerization of the 11-cis-retinylidene chromophore. Upon warming, bathopinopsin decayed through a series of photobleaching intermediates: lumipinopsin (lambda(max) 461 nm), metapinopsin I (460 nm), metapinopsin II (385 nm), and metapinopsin III (460 nm). Biochemical and kinetic analyses showed that metapinopsin II is a physiologically important photoproduct activating transducin. Detailed kinetic analyses revealed that the formation of metapinopsin II is as fast as that of a chicken cone pigment, green, but that the decay process of metapinopsin II is as slow as that of the rod pigment, rhodopsin. These results indicate that pinopsin is a new type of pigment with a chimeric nature between rod and cone visual pigments in terms of the thermal behaviors of the meta II intermediate. Such a long-lived active state of pinopsin may play a role in the pineal-specific phototransduction process.
authors.affiliation: Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Hongo, Bunkyo-Ku, Tokyo 113-0033, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Nakamura
authors.forename: D
authors.initials: D
authors.lastname: Kojima
authors.forename: H
authors.initials: H
authors.lastname: Imai
authors.forename: A
authors.initials: A
authors.lastname: Terakita
authors.forename: T
authors.initials: T
authors.lastname: Okano
authors.forename: Y
authors.initials: Y
authors.lastname: Shichida
authors.forename: Y
authors.initials: Y
authors.lastname: Fukada
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D030161:Avian Proteins; D001483:Base Sequence; D002417:Cattle; D002645:Chickens; D006639:Histidine; D007536:Isomerism; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D010777:Photochemistry; D020419:Photoreceptor Cells, Vertebrate / Q000737:chemistry*; D010870:Pineal Gland / Q000737:chemistry; D012243:Rhodopsin / Q000031:analogs & derivatives / Q000378:metabolism; D017299:Rod Opsins / Q000737:chemistry* / Q000378:metabolism; D015293:Transducin / Q000378:metabolism
chemical_list: D030161:Avian Proteins; D006639:Histidine; D009419:Nerve Tissue Proteins; D012243:Rhodopsin; D017299:Rod Opsins; D015293:Transducin; C090139:OPNP protein, chicken; C013110:metarhodopsins