Study on the dynamic structure change of membrane supramolecular flagellar motor and the force generation

2014 Fiscal Year Final Research Report

• Project/Area Number: 23247024
• Research Category: Grant-in-Aid for Scientific Research (A)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Biophysics
• Research Institution: Nagoya University
• Principal Investigator: HOMMA Michio 名古屋大学, 理学(系)研究科(研究院), 教授 (50209342)
• Co-Investigator(Kenkyū-buntansha): KAWAGISHI Ikurou 法政大学, 生命科学部, 教授 (80234037)
• Project Period (FY): 2011-04-01 – 2015-03-31
• Keywords: 生体エネルギー変換 / PomA / PomB / モーター / べん毛 / 膜タンパク質

Outline of Final Research Achievements

The dynamic structural change of the stator in the sodium-driven flagellar motor of Vibrio was analyzed for the mechanism of rotational energy conversion when the coupling ions flow in the stator of the motor. The ion uptake activity by the stator has been detected directly and firstly in vivo by atomic absorption analysis. In addition, although in Vibrio stator the mutation of the ion binding residues, PomB-D24N, give completely nonfunctional penotype, the additional PomA-N194D mutation suppress the defect. It is inferred that the ion binding capacity was recovered by the mutation. Furthermor, the structure of the C-terminal fragment of PomB (PomBC) was determined by crystallographic analysis and was compared with the structure of the correponding region of E. coli MotB. Based on these structural information chimeric proteins PotB made of PomB and MotB were constrected and carried out the functional analysis of these chimeric proteins.

Free Research Field

生物物理学