Chimeric nature of pinopsin between rod and cone visual pigments

Atsushi Nakamura, Daisuke Kojima, Hiroo Imai, Akihisa Terakita, Toshiyuki Okano, Yoshinori Shichida, Yoshitaka Fukada

Research output: Contribution to journalArticle

33 Citations (Scopus)

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°C), we detected two kinds of photoproducts, bathopinopsin and isopinopsin, having their absorption maxima (λ(max)) at 527 and ~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 (λ(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.

Original languageEnglish
Pages (from-to)14738-14745
Number of pages8
JournalBiochemistry
Volume38
Issue number45
DOIs
Publication statusPublished - 1999 Nov 9
Externally publishedYes

Fingerprint

Vertebrate Photoreceptor Cells
Retinal Pigments
Rhodopsin
Pigments
Transducin
Cones
Chickens
Rod Opsins
Cone Opsins
Light Signal Transduction
Retinal Cone Photoreceptor Cells
Opsins
Photobleaching
Retinal Rod Photoreceptor Cells
Temperature
Photons
Kinetics
Spectrum Analysis
Liquid nitrogen
Nitrogen

ASJC Scopus subject areas

  • Biochemistry

Cite this

Nakamura, A., Kojima, D., Imai, H., Terakita, A., Okano, T., Shichida, Y., & Fukada, Y. (1999). Chimeric nature of pinopsin between rod and cone visual pigments. Biochemistry, 38(45), 14738-14745. https://doi.org/10.1021/bi9913496

Chimeric nature of pinopsin between rod and cone visual pigments. / Nakamura, Atsushi; Kojima, Daisuke; Imai, Hiroo; Terakita, Akihisa; Okano, Toshiyuki; Shichida, Yoshinori; Fukada, Yoshitaka.

In: Biochemistry, Vol. 38, No. 45, 09.11.1999, p. 14738-14745.

Research output: Contribution to journalArticle

Nakamura, A, Kojima, D, Imai, H, Terakita, A, Okano, T, Shichida, Y & Fukada, Y 1999, 'Chimeric nature of pinopsin between rod and cone visual pigments', Biochemistry, vol. 38, no. 45, pp. 14738-14745. https://doi.org/10.1021/bi9913496
Nakamura A, Kojima D, Imai H, Terakita A, Okano T, Shichida Y et al. Chimeric nature of pinopsin between rod and cone visual pigments. Biochemistry. 1999 Nov 9;38(45):14738-14745. https://doi.org/10.1021/bi9913496
Nakamura, Atsushi ; Kojima, Daisuke ; Imai, Hiroo ; Terakita, Akihisa ; Okano, Toshiyuki ; Shichida, Yoshinori ; Fukada, Yoshitaka. / Chimeric nature of pinopsin between rod and cone visual pigments. In: Biochemistry. 1999 ; Vol. 38, No. 45. pp. 14738-14745.
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