マイコプラズマの滑走運動に必要なモーターの分子構造を世界で初めて明らかに!

2025-03-04 大阪公立大学

<関連情報>

• https://www.omu.ac.jp/info/research_news/entry-16557.html
• https://www.omu.ac.jp/assets/attachmentfile/attachmentfile-file-66568.pdf
• https://www.science.org/doi/10.1126/sciadv.adr9319

マイコプラズマの滑空運動におけるF1様ATPaseの二量体形成 Dimeric assembly of F1-like ATPase for the gliding motility of Mycoplasma

Takuma Toyonaga, Takayuki Kato, Akihiro Kawamoto, Tomoko Miyata, […], and Makoto Miyata
Science Advances  Published:26 Feb 2025

Abstract

Rotary ATPases, including F₁F_O-, V₁V_O-, and A₁A_O-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, Mycoplasma mobile, a dimeric F₁-like ATPase forms a chain structure within the cell, which is proposed to drive the gliding motility. However, the mechanisms of force generation and transmission remain unclear. We determined the electron cryomicroscopy (cryo-EM) structure of the dimeric F₁-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F₁F_O-ATPases. The F₁-like ATPase unit associated by two subunits GliD and GliE was named G₁-ATPase as an R₁ domain of rotary ATPases. G₁-β subunit, a homolog of the F₁-ATPase catalytic subunit, exhibited a specific N-terminal region that incorporates the glycolytic enzyme, phosphoglycerate kinase into the complex. Structural features of the ATPase displayed strong similarities to F₁-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G₁-ATPase drives the Mycoplasma gliding motility.