Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists

Sampreeth Thayyil; Yukinori Nishigami; Md Jahirul Islam; P K Hashim; Ken'ya Furuta; Kazuhiro Oiwa; Jian Yu; Min Yao; Toshiyuki Nakagaki; Nobuyuki Tamaoki

doi:10.1002/chem.202200807

Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists

Chemistry. 2022 May 25;28(30):e202200807. doi: 10.1002/chem.202200807. Epub 2022 Apr 12.

Authors

Sampreeth Thayyil^{1

2}, Yukinori Nishigami^{1

2}, Md Jahirul Islam^{1

2

3}, P K Hashim^{1

2}, Ken'ya Furuta⁴, Kazuhiro Oiwa⁴, Jian Yu⁵, Min Yao⁵, Toshiyuki Nakagaki^{1

2}, Nobuyuki Tamaoki^{1

2}

Affiliations

¹ Research Institute for Electronic Science, Hokkaido University, Kita20, Nishi 10, Kita-ku, Sapporo, Hokkaido, 001-0020, Japan.
² Graduate School of Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo, Hokkaido, 060-0810, Japan.
³ Current Address: Institute of Science and Technology Austria, 3400, Klosterneuburg, Austria.
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.

PMID: 35332959
DOI: 10.1002/chem.202200807

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: ATP antagonist; azobenzene; dynein; motor protein; photocontrol.

MeSH terms

Adenosine Triphosphate* / metabolism
Binding Sites
Cytoplasm / metabolism
Dyneins* / chemistry
Dyneins* / metabolism
Microtubules

Substances

Adenosine Triphosphate
Dyneins

Abstract

MeSH terms

Substances

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