Chained Structure of Dimeric F 1 -like ATPase in Mycoplasma mobile Gliding Machinery-Reference-Cited by-同舟云学术

Chained Structure of Dimeric F 1 -like ATPase in Mycoplasma mobile Gliding Machinery

Published:2021-08-31 Issue:4 Volume:12 Page:
ISSN:2150-7511
Container-title:mBio
language:en
Short-container-title:mBio

Author:

Toyonaga Takuma¹^ORCID,Kato Takayuki²^ORCID,Kawamoto Akihiro²^ORCID,Kodera Noriyuki³^ORCID,Hamaguchi Tasuku¹⁴^ORCID,Tahara Yuhei O.¹⁴^ORCID,Ando Toshio³^ORCID,Namba Keiichi⁵⁶⁷^ORCID,Miyata Makoto¹⁴^ORCID

Affiliation:

1. Graduate School of Science, Osaka City University, Osaka, Osaka, Japan

2. Institute for Protein Research, Osaka University, Suita, Osaka, Japan

3. Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa, Japan

4. The OCU Advanced Research Institute for Natural Science and Technology (OCARINA), Osaka City University, Osaka, Osaka, Japan

5. Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan

6. RIKEN Center for Biosystems Dynamics Research, SPring-8 Center, Suita, Osaka, Japan

7. JEOL YOKOGUSHI Research Alliance Laboratories, Osaka University, Suita, Osaka, Japan

Abstract

F 1 F o -ATPase, a rotary ATPase, is widespread in the membranes of mitochondria, chloroplasts, and bacteria and converts ATP energy with a proton motive force across the membrane by its physical rotation. Homologous protein complexes play roles in ion and protein transport. Mycoplasma mobile , a pathogenic bacterium, was recently suggested to have a special motility system evolutionarily derived from F 1 -ATPase.

Funder

Ministry of Education, Culture, Sports, Science and Technology

MEXT | Japan Science and Technology Agency

Osaka City University

Sumitomo Mitsui Trust Bank

MEXT | Japan Society for the Promotion of Science

Japan Agency for Medical Research and Development

JEOL

Publisher

American Society for Microbiology

Subject

Virology,Microbiology