Journal
SCIENCE
Volume 333, Issue 6043, Pages 755-758Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1205510
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Funding
- Ministry of Education, Culture, Sports, Science and Technology [18074005, 18201025, 21770168, 21681017, 2102301, 21107517, 22247025, 20221006]
- Knowledge Cluster Initiative
- Japan Science and Technology Agency for Core Research for Evolutional Science and Technology
- Grants-in-Aid for Scientific Research [18201025, 21681017, 20221006, 21770168, 22247025, 21107517, 22018018, 21113002] Funding Source: KAKEN
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F-1 is an adenosine triphosphate (ATP)-driven motor in which three torque-generating beta subunits in the alpha(3)beta(3) stator ring sequentially undergo conformational changes upon ATP hydrolysis to rotate the central shaft gamma unidirectionally. Although extensive experimental and theoretical work has been done, the structural basis of cooperative torque generation to realize the unidirectional rotation remains elusive. We used high-speed atomic force microscopy to show that the rotorless F-1 still rotates; in the isolated alpha(3)beta(3) stator ring, the three beta subunits cyclically propagate conformational states in the counterclockwise direction, similar to the rotary shaft rotation in F-1. The structural basis of unidirectionality is programmed in the stator ring. These findings have implications for cooperative interplay between subunits in other hexameric ATPases.
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