A non-mammalian type opsin 5 functions dually in the photoreceptive and non-photoreceptive organs of birds

Hideyo Ohuchi, Takahiro Yamashita, Sayuri Tomonari, Sari Fujita-Yanagibayashi, Kazumi Sakai, Sumihare Noji, Yoshinori Shichida

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

A mammalian type opsin 5 (neuropsin) is a recently identified ultraviolet (UV)-sensitive pigment of the retina and other photosensitive organs in birds. Two other opsin 5-related molecules have been found in the genomes of non-mammalian vertebrates. However, their functions have not been examined as yet. Here, we identify the molecular properties of a second avian opsin 5, cOpn5L2 (chicken opsin 5-like 2), and its localization in the post-hatch chicken. Spectrophotometric analysis and radionucleotide-binding assay have revealed that cOpn5L2 is a UV-sensitive bistable pigment that couples with the Gi subtype of guanine nucleotide-binding protein (G protein). As a bistable pigment, it also shows the direct binding ability to agonist all-trans-retinal to activate G protein. The absorption maxima of UV-light-absorbing and visible light-absorbing forms were 350 and 521 nm, respectively. Expression analysis showed relatively high expression of cOpn5L2 mRNA in the adrenal gland, which is not photoreceptive but an endocrine organ, while lower expression was found in the brain and retina. At the protein level, cOpn5L2 immunoreactive cells were present in the chromaffin cells of the adrenal gland. In the brain, cOpn5L2 immunoreactive cells were found in the paraventricular and supraoptic nuclei of the anterior hypothalamus, known for photoreceptive deep brain areas. In the retina, cOpn5L2 protein was localized to subsets of cells in the ganglion cell layer and the inner nuclear layer. These results suggest that the non-mammalian type opsin 5 (Opn5L2) functions as a second UV sensor in the photoreceptive organs, while it might function as chemosensor using its direct binding ability to agonist all-trans-retinal in non-photoreceptive organs such as the adrenal gland of birds.

Original languageEnglish
Article numbere31534
JournalPLoS One
Volume7
Issue number2
DOIs
Publication statusPublished - Feb 14 2012
Externally publishedYes

Fingerprint

Opsins
opsin
Birds
Chickens
birds
chickens
adrenal glands
Adrenal Glands
retina
Pigments
Retina
Brain
pigments
binding capacity
G-proteins
brain
GTP-Binding Proteins
agonists
Anterior Hypothalamic Nucleus
cells

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Ohuchi, H., Yamashita, T., Tomonari, S., Fujita-Yanagibayashi, S., Sakai, K., Noji, S., & Shichida, Y. (2012). A non-mammalian type opsin 5 functions dually in the photoreceptive and non-photoreceptive organs of birds. PLoS One, 7(2), [e31534]. https://doi.org/10.1371/journal.pone.0031534

A non-mammalian type opsin 5 functions dually in the photoreceptive and non-photoreceptive organs of birds. / Ohuchi, Hideyo; Yamashita, Takahiro; Tomonari, Sayuri; Fujita-Yanagibayashi, Sari; Sakai, Kazumi; Noji, Sumihare; Shichida, Yoshinori.

In: PLoS One, Vol. 7, No. 2, e31534, 14.02.2012.

Research output: Contribution to journalArticle

Ohuchi, H, Yamashita, T, Tomonari, S, Fujita-Yanagibayashi, S, Sakai, K, Noji, S & Shichida, Y 2012, 'A non-mammalian type opsin 5 functions dually in the photoreceptive and non-photoreceptive organs of birds', PLoS One, vol. 7, no. 2, e31534. https://doi.org/10.1371/journal.pone.0031534
Ohuchi, Hideyo ; Yamashita, Takahiro ; Tomonari, Sayuri ; Fujita-Yanagibayashi, Sari ; Sakai, Kazumi ; Noji, Sumihare ; Shichida, Yoshinori. / A non-mammalian type opsin 5 functions dually in the photoreceptive and non-photoreceptive organs of birds. In: PLoS One. 2012 ; Vol. 7, No. 2.
@article{dd1631cdb7264e8c9a79e75b421e500e,
title = "A non-mammalian type opsin 5 functions dually in the photoreceptive and non-photoreceptive organs of birds",
abstract = "A mammalian type opsin 5 (neuropsin) is a recently identified ultraviolet (UV)-sensitive pigment of the retina and other photosensitive organs in birds. Two other opsin 5-related molecules have been found in the genomes of non-mammalian vertebrates. However, their functions have not been examined as yet. Here, we identify the molecular properties of a second avian opsin 5, cOpn5L2 (chicken opsin 5-like 2), and its localization in the post-hatch chicken. Spectrophotometric analysis and radionucleotide-binding assay have revealed that cOpn5L2 is a UV-sensitive bistable pigment that couples with the Gi subtype of guanine nucleotide-binding protein (G protein). As a bistable pigment, it also shows the direct binding ability to agonist all-trans-retinal to activate G protein. The absorption maxima of UV-light-absorbing and visible light-absorbing forms were 350 and 521 nm, respectively. Expression analysis showed relatively high expression of cOpn5L2 mRNA in the adrenal gland, which is not photoreceptive but an endocrine organ, while lower expression was found in the brain and retina. At the protein level, cOpn5L2 immunoreactive cells were present in the chromaffin cells of the adrenal gland. In the brain, cOpn5L2 immunoreactive cells were found in the paraventricular and supraoptic nuclei of the anterior hypothalamus, known for photoreceptive deep brain areas. In the retina, cOpn5L2 protein was localized to subsets of cells in the ganglion cell layer and the inner nuclear layer. These results suggest that the non-mammalian type opsin 5 (Opn5L2) functions as a second UV sensor in the photoreceptive organs, while it might function as chemosensor using its direct binding ability to agonist all-trans-retinal in non-photoreceptive organs such as the adrenal gland of birds.",
author = "Hideyo Ohuchi and Takahiro Yamashita and Sayuri Tomonari and Sari Fujita-Yanagibayashi and Kazumi Sakai and Sumihare Noji and Yoshinori Shichida",
year = "2012",
month = "2",
day = "14",
doi = "10.1371/journal.pone.0031534",
language = "English",
volume = "7",
journal = "PLoS One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "2",

}

TY - JOUR

T1 - A non-mammalian type opsin 5 functions dually in the photoreceptive and non-photoreceptive organs of birds

AU - Ohuchi, Hideyo

AU - Yamashita, Takahiro

AU - Tomonari, Sayuri

AU - Fujita-Yanagibayashi, Sari

AU - Sakai, Kazumi

AU - Noji, Sumihare

AU - Shichida, Yoshinori

PY - 2012/2/14

Y1 - 2012/2/14

N2 - A mammalian type opsin 5 (neuropsin) is a recently identified ultraviolet (UV)-sensitive pigment of the retina and other photosensitive organs in birds. Two other opsin 5-related molecules have been found in the genomes of non-mammalian vertebrates. However, their functions have not been examined as yet. Here, we identify the molecular properties of a second avian opsin 5, cOpn5L2 (chicken opsin 5-like 2), and its localization in the post-hatch chicken. Spectrophotometric analysis and radionucleotide-binding assay have revealed that cOpn5L2 is a UV-sensitive bistable pigment that couples with the Gi subtype of guanine nucleotide-binding protein (G protein). As a bistable pigment, it also shows the direct binding ability to agonist all-trans-retinal to activate G protein. The absorption maxima of UV-light-absorbing and visible light-absorbing forms were 350 and 521 nm, respectively. Expression analysis showed relatively high expression of cOpn5L2 mRNA in the adrenal gland, which is not photoreceptive but an endocrine organ, while lower expression was found in the brain and retina. At the protein level, cOpn5L2 immunoreactive cells were present in the chromaffin cells of the adrenal gland. In the brain, cOpn5L2 immunoreactive cells were found in the paraventricular and supraoptic nuclei of the anterior hypothalamus, known for photoreceptive deep brain areas. In the retina, cOpn5L2 protein was localized to subsets of cells in the ganglion cell layer and the inner nuclear layer. These results suggest that the non-mammalian type opsin 5 (Opn5L2) functions as a second UV sensor in the photoreceptive organs, while it might function as chemosensor using its direct binding ability to agonist all-trans-retinal in non-photoreceptive organs such as the adrenal gland of birds.

AB - A mammalian type opsin 5 (neuropsin) is a recently identified ultraviolet (UV)-sensitive pigment of the retina and other photosensitive organs in birds. Two other opsin 5-related molecules have been found in the genomes of non-mammalian vertebrates. However, their functions have not been examined as yet. Here, we identify the molecular properties of a second avian opsin 5, cOpn5L2 (chicken opsin 5-like 2), and its localization in the post-hatch chicken. Spectrophotometric analysis and radionucleotide-binding assay have revealed that cOpn5L2 is a UV-sensitive bistable pigment that couples with the Gi subtype of guanine nucleotide-binding protein (G protein). As a bistable pigment, it also shows the direct binding ability to agonist all-trans-retinal to activate G protein. The absorption maxima of UV-light-absorbing and visible light-absorbing forms were 350 and 521 nm, respectively. Expression analysis showed relatively high expression of cOpn5L2 mRNA in the adrenal gland, which is not photoreceptive but an endocrine organ, while lower expression was found in the brain and retina. At the protein level, cOpn5L2 immunoreactive cells were present in the chromaffin cells of the adrenal gland. In the brain, cOpn5L2 immunoreactive cells were found in the paraventricular and supraoptic nuclei of the anterior hypothalamus, known for photoreceptive deep brain areas. In the retina, cOpn5L2 protein was localized to subsets of cells in the ganglion cell layer and the inner nuclear layer. These results suggest that the non-mammalian type opsin 5 (Opn5L2) functions as a second UV sensor in the photoreceptive organs, while it might function as chemosensor using its direct binding ability to agonist all-trans-retinal in non-photoreceptive organs such as the adrenal gland of birds.

UR - http://www.scopus.com/inward/record.url?scp=84856866305&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84856866305&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0031534

DO - 10.1371/journal.pone.0031534

M3 - Article

C2 - 22348098

AN - SCOPUS:84856866305

VL - 7

JO - PLoS One

JF - PLoS One

SN - 1932-6203

IS - 2

M1 - e31534

ER -