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A dynein-associated photoreceptor protein prevents ciliary acclimation to blue light

Sci Adv. 2021-02; 
Osamu Kutomi, Ryosuke Yamamoto, Keiko Hirose, Katsutoshi Mizuno, Yuuhei Nakagiri, Hiroshi Imai, Akira Noga, Jagan Mohan Obbineni, Noemi Zimmermann, Masako Nakajima, Daisuke Shibata, Misa Shibata, Kogiku Shiba, Masaki Kita, Hideo Kigoshi, Yui Tanaka, Yuya Yamasaki, Yuma Asahina, Chihong Song, Mami Nomura, Mamoru Nomura, Ayako Nakajima, Mia Nakachi, Lixy Yamada, Shiori Nakazawa, Hitoshi Sawada, Kazuyoshi Murata, Kaoru Mitsuoka, Takashi Ishikawa, Ken-Ichi Wakabayashi, Takahide Kon, Kazuo Inaba
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Custom Vector Construction the synthesized WT MOT7 cDNA sequence (GenScript Japan) was cloned into the Nde I/Bam HI sites of the Chlamydomonas expression vector pIC2L-MCS-BCCP-3HA-Hyg (a gift from H. Yanagisawa, The University of Tokyo) Get A Quote

摘要

Light-responsive regulation of ciliary motility is known to be conducted through modulation of dyneins, but the mechanism is not fully understood. Here, we report a novel subunit of the two-headed f/I1 inner arm dynein, named DYBLUP, in animal spermatozoa and a unicellular green alga. This subunit contains a BLUF (sensors of blue light using FAD) domain that appears to directly modulate dynein activity in response to light. DYBLUP (dynein-associated BLUF protein) mediates the connection between the f/I1 motor domain and the tether complex that links the motor to the doublet microtubule. lacking the DYBLUP ortholog shows both positive and negative phototaxis but becomes acclimated and attracted to high-intensit... More

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