ヨコヤマ ケン   YOKOYAMA KEN
  横山 謙
   所属   京都産業大学  生命科学部 先端生命科学科
   職種   教授
言語種別 英語
発行・発表の年月 2013/05
形態種別 研究論文
査読 査読あり
標題 Common Evolutionary Origin for the Rotor Domain of Rotary Atpases and Flagellar Protein Export Apparatus
執筆形態 その他
掲載誌名 PLOS ONE
出版社・発行元 PUBLIC LIBRARY SCIENCE
巻・号・頁 8(5),pp.e64695
著者・共著者 Jun-ichi Kishikawa,Tatsuya Ibuki,Shuichi Nakamura,Astuko Nakanishi,Tohru Minamino,Tomoko Miyata,Keiichi Namba,Hiroki Konno,Hiroshi Ueno,Katsumi Imada,Ken Yokoyama
概要 The V-1-and F-1-rotary ATPases contain a rotor that rotates against a catalytic A(3)B(3) or alpha(3)beta(3) stator. The rotor F-1-gamma or V-1-DF is composed of both anti-parallel coiled coil and globular-loop parts. The bacterial flagellar type III export apparatus contains a V-1/F-1-like ATPase ring structure composed of FliI6 homo-hexamer and FliJ which adopts an anti-parallel coiled coil structure without the globular-loop part. Here we report that FliJ of Salmonella enterica serovar Typhimurium shows a rotor like function in Thermus thermophilus A(3)B(3) based on both biochemical and structural analysis. Single molecular analysis indicates that an anti-parallel coiled-coil structure protein (FliJ structure protein) functions as a rotor in A(3)B(3). A rotary ATPase possessing an F-1-gamma-like protein generated by fusion of the D and F subunits of V-1 rotates, suggesting F-1-gamma could be the result of a fusion of the genes encoding two separate rotor subunits. Together with sequence comparison among the globular part proteins, the data strongly suggest that the rotor domains of the rotary ATPases and the flagellar export apparatus share a common evolutionary origin.
DOI 10.1371/journal.pone.0064695
ISSN 1932-6203
PMID 23724081