Light-dependent structural change of chicken retinal cryptochrome4

Ryuji Watari, Chiaki Yamaguchi, Wataru Zemba, Yoko Kubo, Keiko Okano, Toshiyuki Okano

    Research output: Contribution to journalArticle

    28 Citations (Scopus)

    Abstract

    Animals have several classes of cryptochromes (CRYs), some of which function as core elements of circadian clockwork, circadian photoreceptors, and/or light-dependent magnetoreceptors. In addition to the circadian clock genes Cry1 and Cry2, nonmammalian vertebrates have the Cry4 gene, the molecular function of which remains unknown. Here we analyzed chicken CRY4 (cCRY4) expression in the retina with in situ hybridization and found that cCRY4 was likely transcribed in the visual pigment cells, cells in the inner nuclear layer, and retinal ganglion cells. We further developed several monoclonal antibodies to the carboxyl-terminal extension of cCRY4 and localized cCRY4 protein with immunohistochemistry. Consistent with the results of in situ hybridization, cCRY4 immunoreactivity was found in visual pigment cells and cells located at the inner nuclear layer and the retinal ganglion cell layer. Among the antibodies, one termed C1-mAb had its epitope within the carboxylterminal 14-amino acid sequence (QLTRDDADDPMEMK) and associated with cCRY4 in the retinal soluble fraction more strongly in the dark than under blue light conditions. Immunoprecipitation experiments under various light conditions indicated that cCRY4 from the immunocomplex formed in the dark dissociated from C1-mAb during blue light illumination as weak as 25 μW/cm2 and that the release occurred with not only blue but also near UV light. These results suggest that cCRY4 reversibly changes its structure within the carboxyl-terminal region in a light-dependent manner and operates as a photoreceptor or magnetoreceptor with short wavelength sensitivity in the retina.

    Original languageEnglish
    Pages (from-to)42634-42641
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume287
    Issue number51
    DOIs
    Publication statusPublished - 2012 Dec 14

    Fingerprint

    Chickens
    Light
    Retinal Pigments
    Genes
    Cryptochromes
    Retinal Ganglion Cells
    In Situ Hybridization
    Retina
    Ultraviolet radiation
    Clocks
    Epitopes
    Animals
    Circadian Clocks
    Lighting
    Monoclonal Antibodies
    Cells
    Ultraviolet Rays
    Amino Acids
    Wavelength
    Immunoprecipitation

    ASJC Scopus subject areas

    • Biochemistry
    • Cell Biology
    • Molecular Biology

    Cite this

    Light-dependent structural change of chicken retinal cryptochrome4. / Watari, Ryuji; Yamaguchi, Chiaki; Zemba, Wataru; Kubo, Yoko; Okano, Keiko; Okano, Toshiyuki.

    In: Journal of Biological Chemistry, Vol. 287, No. 51, 14.12.2012, p. 42634-42641.

    Research output: Contribution to journalArticle

    Watari, R, Yamaguchi, C, Zemba, W, Kubo, Y, Okano, K & Okano, T 2012, 'Light-dependent structural change of chicken retinal cryptochrome4', Journal of Biological Chemistry, vol. 287, no. 51, pp. 42634-42641. https://doi.org/10.1074/jbc.M112.395731
    Watari, Ryuji ; Yamaguchi, Chiaki ; Zemba, Wataru ; Kubo, Yoko ; Okano, Keiko ; Okano, Toshiyuki. / Light-dependent structural change of chicken retinal cryptochrome4. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 51. pp. 42634-42641.
    @article{771f1ca933754424bbf3c448af052ce7,
    title = "Light-dependent structural change of chicken retinal cryptochrome4",
    abstract = "Animals have several classes of cryptochromes (CRYs), some of which function as core elements of circadian clockwork, circadian photoreceptors, and/or light-dependent magnetoreceptors. In addition to the circadian clock genes Cry1 and Cry2, nonmammalian vertebrates have the Cry4 gene, the molecular function of which remains unknown. Here we analyzed chicken CRY4 (cCRY4) expression in the retina with in situ hybridization and found that cCRY4 was likely transcribed in the visual pigment cells, cells in the inner nuclear layer, and retinal ganglion cells. We further developed several monoclonal antibodies to the carboxyl-terminal extension of cCRY4 and localized cCRY4 protein with immunohistochemistry. Consistent with the results of in situ hybridization, cCRY4 immunoreactivity was found in visual pigment cells and cells located at the inner nuclear layer and the retinal ganglion cell layer. Among the antibodies, one termed C1-mAb had its epitope within the carboxylterminal 14-amino acid sequence (QLTRDDADDPMEMK) and associated with cCRY4 in the retinal soluble fraction more strongly in the dark than under blue light conditions. Immunoprecipitation experiments under various light conditions indicated that cCRY4 from the immunocomplex formed in the dark dissociated from C1-mAb during blue light illumination as weak as 25 μW/cm2 and that the release occurred with not only blue but also near UV light. These results suggest that cCRY4 reversibly changes its structure within the carboxyl-terminal region in a light-dependent manner and operates as a photoreceptor or magnetoreceptor with short wavelength sensitivity in the retina.",
    author = "Ryuji Watari and Chiaki Yamaguchi and Wataru Zemba and Yoko Kubo and Keiko Okano and Toshiyuki Okano",
    year = "2012",
    month = "12",
    day = "14",
    doi = "10.1074/jbc.M112.395731",
    language = "English",
    volume = "287",
    pages = "42634--42641",
    journal = "Journal of Biological Chemistry",
    issn = "0021-9258",
    publisher = "American Society for Biochemistry and Molecular Biology Inc.",
    number = "51",

    }

    TY - JOUR

    T1 - Light-dependent structural change of chicken retinal cryptochrome4

    AU - Watari, Ryuji

    AU - Yamaguchi, Chiaki

    AU - Zemba, Wataru

    AU - Kubo, Yoko

    AU - Okano, Keiko

    AU - Okano, Toshiyuki

    PY - 2012/12/14

    Y1 - 2012/12/14

    N2 - Animals have several classes of cryptochromes (CRYs), some of which function as core elements of circadian clockwork, circadian photoreceptors, and/or light-dependent magnetoreceptors. In addition to the circadian clock genes Cry1 and Cry2, nonmammalian vertebrates have the Cry4 gene, the molecular function of which remains unknown. Here we analyzed chicken CRY4 (cCRY4) expression in the retina with in situ hybridization and found that cCRY4 was likely transcribed in the visual pigment cells, cells in the inner nuclear layer, and retinal ganglion cells. We further developed several monoclonal antibodies to the carboxyl-terminal extension of cCRY4 and localized cCRY4 protein with immunohistochemistry. Consistent with the results of in situ hybridization, cCRY4 immunoreactivity was found in visual pigment cells and cells located at the inner nuclear layer and the retinal ganglion cell layer. Among the antibodies, one termed C1-mAb had its epitope within the carboxylterminal 14-amino acid sequence (QLTRDDADDPMEMK) and associated with cCRY4 in the retinal soluble fraction more strongly in the dark than under blue light conditions. Immunoprecipitation experiments under various light conditions indicated that cCRY4 from the immunocomplex formed in the dark dissociated from C1-mAb during blue light illumination as weak as 25 μW/cm2 and that the release occurred with not only blue but also near UV light. These results suggest that cCRY4 reversibly changes its structure within the carboxyl-terminal region in a light-dependent manner and operates as a photoreceptor or magnetoreceptor with short wavelength sensitivity in the retina.

    AB - Animals have several classes of cryptochromes (CRYs), some of which function as core elements of circadian clockwork, circadian photoreceptors, and/or light-dependent magnetoreceptors. In addition to the circadian clock genes Cry1 and Cry2, nonmammalian vertebrates have the Cry4 gene, the molecular function of which remains unknown. Here we analyzed chicken CRY4 (cCRY4) expression in the retina with in situ hybridization and found that cCRY4 was likely transcribed in the visual pigment cells, cells in the inner nuclear layer, and retinal ganglion cells. We further developed several monoclonal antibodies to the carboxyl-terminal extension of cCRY4 and localized cCRY4 protein with immunohistochemistry. Consistent with the results of in situ hybridization, cCRY4 immunoreactivity was found in visual pigment cells and cells located at the inner nuclear layer and the retinal ganglion cell layer. Among the antibodies, one termed C1-mAb had its epitope within the carboxylterminal 14-amino acid sequence (QLTRDDADDPMEMK) and associated with cCRY4 in the retinal soluble fraction more strongly in the dark than under blue light conditions. Immunoprecipitation experiments under various light conditions indicated that cCRY4 from the immunocomplex formed in the dark dissociated from C1-mAb during blue light illumination as weak as 25 μW/cm2 and that the release occurred with not only blue but also near UV light. These results suggest that cCRY4 reversibly changes its structure within the carboxyl-terminal region in a light-dependent manner and operates as a photoreceptor or magnetoreceptor with short wavelength sensitivity in the retina.

    UR - http://www.scopus.com/inward/record.url?scp=84871125571&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=84871125571&partnerID=8YFLogxK

    U2 - 10.1074/jbc.M112.395731

    DO - 10.1074/jbc.M112.395731

    M3 - Article

    C2 - 23095750

    AN - SCOPUS:84871125571

    VL - 287

    SP - 42634

    EP - 42641

    JO - Journal of Biological Chemistry

    JF - Journal of Biological Chemistry

    SN - 0021-9258

    IS - 51

    ER -