Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 28, Issue 30, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.202200807
Keywords
azobenzene; ATP antagonist; dynein; motor protein; photocontrol
Categories
Funding
- KAKENHI [18H02042]
- Cooperative Research Program of the Network Joint Research Center for Materials and Devices from the Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- Dynamic Alliance for Open Innovation Bridging Human, Environment and Materials from MEXT
- Fostering Joint International Research (B) [19KK0180]
- [21H05308]
- [21H05310]
- Grants-in-Aid for Scientific Research [18H02042] Funding Source: KAKEN
Ask authors/readers for more resources
In this study, we developed azobenzene-based photoswitchable ATP antagonists to control the activity of motor proteins cytoplasmic and axonemal dyneins. Our ATP antagonists showed reversible photoswitching of cytoplasmic dynein activity and regulated axonemal dynein motor activity in a force generation model.
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available