関: cryptochrome

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/06/27 11:14:00」(JST)

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Phototropins are photoreceptor proteins (specifically, flavoproteins) that mediate phototropism responses in higher plants. Along with cryptochromes and phytochromes they allow plants to respond and alter their growth in response to the light environment. Phototropins may also be important for the opening of stomata.

Phototropins are autophosphorylating protein kinases that activate in response to blue light. When blue light hits the phototropin protein in the cell membrane, the phototropin protein will unfold and undergo phosphorylation that can cause a cascade of events inside of the cell.

Phototropins are part of the phototropic sensory system in plants that causes various environmental responses in plants. Phototropins specifically will cause stems to bend towards light, and stomata to open. Also, phototropins are important in chloroplast movements inside the cell. They also mediate the first changes in stem elongation in blue light (before cryptochromes become active) and phototropin 1 also is required for blue light mediated transcript destabilization of specific mRNAs in the cell.

References[edit]

Briggs WR, Olney MA (January 2001). "Photoreceptors in plant photomorphogenesis to date. Five phytochromes, two cryptochromes, one phototropin, and one superchrome". Plant Physiol. 125 (1): 85–8. PMC 1539332. PMID 11154303.
Wada M, Kagawa T, Sato Y (2003). "Chloroplast movement". Annu Rev Plant Biol 54: 455–68. doi:10.1146/annurev.arplant.54.031902.135023. PMID 14502999.
DeBlasio SL, Luesse DL, Hangarter RP (September 2005). "A plant-specific protein essential for blue-light-induced chloroplast movements". Plant Physiol. 139 (1): 101–14. doi:10.1104/pp.105.061887. PMC 1203361. PMID 16113226.
Peter E, Dick B, Baeurle SA (2010). "Mechanism of signal transduction of the LOV2-Jα photosensor from Avena sativa". Nat Commun 1: 122. doi:10.1038/ncomms1121. PMID 21081920.

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English Journal

Chloroplast movement.

Wada M.SourceBiology Department, Faculty of Science, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan. Electronic address: wadascb@kyushu-u.org.
Plant science : an international journal of experimental plant biology.Plant Sci.2013 Sep;210:177-82. doi: 10.1016/j.plantsci.2013.05.016. Epub 2013 Jun 7.
Chloroplast movement is important for plant survival under high light and for efficient photosynthesis under low light. This review introduces recent knowledge on chloroplast movement and shows how to analyze the responses and the moving mechanisms, potentially inspiring research in this field. Avoi
PMID 23849124

Oxygen-Dependent Photochemistry and Photophysics of "MiniSOG," a Protein-Encased Flavin.

Pimenta FM, Jensen RL, Breitenbach T, Etzerodt M, Ogilby PR.SourceDepartment of Chemistry, Center for Oxygen Microscopy and Imaging, Aarhus University, Aarhus, Denmark.
Photochemistry and photobiology.Photochem Photobiol.2013 Jul 19. doi: 10.1111/php.12111. [Epub ahead of print]
Selected photochemical and photophysical parameters of flavin mononucleotide (FMN) have been examined under conditions in which FMN is (1) solvated in a buffered aqueous solution, and (2) encased in a protein likewise solvated in a buffered aqueous solution. The latter was achieved using the so-call
PMID 23869989

The amino acids surrounding the flavin 7a-methyl group determine the UVA spectral features of a LOV protein.

Raffelberg S, Gutt A, Gärtner W, Mandalari C, Abbruzzetti S, Viappiani C, Losi A.AbstractAbstract Flavin-binding LOV domains (LOV, light, oxygen, voltage) are UVA/Blue-light sensing protein units that form upon light induction a reversible flavin mononucleotide (FMN)-cysteine adduct. In their dark-adapted state LOV domains exhibit the typical spectral features of fully oxidized riboflavin derivatives. A survey on the absorption spectra of various LOV domains revealed that the UVA spectral range is the most variable region (whereas the absorption band at 450 nm is virtually unchanged), showing essentially two distinct patterns found in plant phototropin LOV1 and LOV2 domains respectively. In this work we have identified a residue directly interacting with the isoalloxazine methyl group at C(7a), as the major UVA spectral tuner. In YtvA from Bacillus subtilis this amino acid is threonine 30 and its mutation into apolar residues converts the LOV2-like spectrum of native YtvA into a LOV1-like pattern. Mutation T30A also accelerates the photocycle ca. 4-fold. Together with control mutations at different positions, our results experimentally confirm the previously calculated direction of the transition dipole moment for the UVA ππ* state and identify mechanisms underlying spectral tuning in LOV domains.
Biological chemistry.Biol Chem.2013 Jul 4. pii: /j/bchm.just-accepted/hsz-2013-0163/hsz-2013-0163.xml. doi: 10.1515/hsz-2013-0163. [Epub ahead of print]
Abstract Flavin-binding LOV domains (LOV, light, oxygen, voltage) are UVA/Blue-light sensing protein units that form upon light induction a reversible flavin mononucleotide (FMN)-cysteine adduct. In their dark-adapted state LOV domains exhibit the typical spectral features of fully oxidized riboflav
PMID 23828427

Japanese Journal

紫外光から遠赤色光まで，多様な植物光受容体

德富哲,岡島公司,吉原静恵
生物物理 55(4), 181-186, 2015
… Phototropin, a member of LOV blue light receptor families, serves to maximize photosynthetic activities by regulating phototropic responses, chloroplast movements, stomata opening, etc. …
NAID 130005090036

2P075 青色光センサータンパク質フォトトロピン1 LOV2ドメインの光反応に対するクラウディング効果(01D. 蛋白質:機能,ポスター,第52回日本生物物理学会年会(2014年度))

Yoshitake Tomoyuki,Nakasone Yusuke,Toyooka Tsuguyoshi,Zikihara Kazunori,Tokutomi Satoru,Terazima Masahide
生物物理 54(SUPPLEMENT_1-2), S207, 2014-08-20
NAID 110009932621