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Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists |
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| Authors: | Sampreeth Thayyil Yukinori Nishigami Md Jahirul Islam P K Hashim Ken'ya Furuta Kazuhiro Oiwa Jian Yu Min Yao Toshiyuki Nakagaki Nobuyuki Tamaoki |
| Institution: | 1. Research Institute for Electronic Science, Hokkaido University, Kita20, Nishi 10, Kita-ku, Sapporo, Hokkaido, 001-0020 Japan
Graduate School of Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo, Hokkaido, 060-0810 Japan These authors contributed equally to this work.;2. Research Institute for Electronic Science, Hokkaido University, Kita20, Nishi 10, Kita-ku, Sapporo, Hokkaido, 001-0020 Japan Graduate School of Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo, Hokkaido, 060-0810 Japan Current Address: Institute of Science and Technology Austria, 3400 Klosterneuburg, Austria;3. Research Institute for Electronic Science, Hokkaido University, Kita20, Nishi 10, Kita-ku, Sapporo, Hokkaido, 001-0020 Japan;4. Advanced ICT Research Institute, National Institute of Information and Communications Technology, Kobe, Hyogo, 651-2492 Japan;5. Faculty of Advanced Life Science, Hokkaido University, North 10 West 8, Kita-ku, Sapporo, Hokkaido, 060-0810 Japan |
| Abstract: | Adenosine triphosphate (ATP) is the energy source for various biochemical processes and biomolecular motors in living things. Development of ATP antagonists and their stimuli-controlled actions offer a novel approach to regulate biological processes. Herein, we developed azobenzene-based photoswitchable ATP antagonists for controlling the activity of motor proteins; cytoplasmic and axonemal dyneins. The new ATP antagonists showed reversible photoswitching of cytoplasmic dynein activity in an in vitro dynein-microtubule system due to the trans and cis photoisomerization of their azobenzene segment. Importantly, our ATP antagonists reversibly regulated the axonemal dynein motor activity for the force generation in a demembranated model of Chlamydomonas reinhardtii. We found that the trans and cis isomers of ATP antagonists significantly differ in their affinity to the ATP binding site. |
| Keywords: | azobenzene ATP antagonist dynein motor protein photocontrol |