Tight Chemomechanical Coupling of the F Motor Relies on Structural Stability

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2020 Jun 13

PMID 32531205

Citations 1

Authors

Mana Tanaka

Tomohiro Kawakami

Tomoaki Okaniwa

Yohei Nakayama

Shoichi Toyabe

Hiroshi Ueno

Eiro Muneyuki

Affiliations

Soon will be listed here.

Abstract

The F motor is a rotating molecular motor that ensures a tight chemomechanical coupling between ATP hydrolysis/synthesis reactions and rotation steps. However, the mechanism underlying this tight coupling remains to be elucidated. In this study, we used electrorotation in single-molecule experiments using an FβE190D mutant to demonstrate that the stall torque was significantly smaller than the wild-type F, indicating a loose coupling of this mutant, despite showing similar stepping torque as the wild-type. Experiments on the ATPase activity after heat treatment and gel filtration of the αβ-subcomplex revealed the unstable structure of the βE190D mutant. Our results suggest that the tight chemomechanical coupling of the F motor relies on the structural stability of F. We also discuss the difference between the stepping torque and the stall torque.

Citing Articles

Physical pictures of rotation mechanisms of F- and V-ATPases: Leading roles of translational, configurational entropy of water.

Yasuda S, Hayashi T, Murata T, Kinoshita M Front Mol Biosci. 2023; 10:1159603.

PMID: 37363397 PMC: 10288849. DOI: 10.3389/fmolb.2023.1159603.

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