BIOPHYSICS
Online ISSN : 1349-2942
ISSN-L : 1349-2942
Regular Article
Expression, purification and biochemical characterization of the cytoplasmic loop of PomA, a stator component of the Na+ driven flagellar motor
Rei Abe YoshizumiShiori KobayashiMizuki GoharaKokoro HayashiChojiro KojimaSeiji KojimaYuki SudoYasuo AsamiMichio Homma
Author information
JOURNAL FREE ACCESS

2013 Volume 9 Pages 21-29

Details
Abstract

Flagellar motors embedded in bacterial membranes are molecular machines powered by specific ion flows. Each motor is composed of a stator and a rotor and the interactions of those components are believed to generate the torque. Na+ influx through the PomA/PomB stator complex of Vibrio alginolyticus is coupled to torque generation and is speculated to trigger structural changes in the cytoplasmic domain of PomA that interacts with a rotor protein in the C-ring, FliG, to drive the rotation. In this study, we tried to overproduce the cytoplasmic loop of PomA (PomA-Loop), but it was insoluble. Thus, we made a fusion protein with a small soluble tag (GB1) which allowed us to express and characterize the recombinant protein. The structure of the PomA-Loop seems to be very elongated or has a loose tertiary structure. When the PomA-Loop protein was produced in E. coli, a slight dominant effect was observed on motility. We conclude that the cytoplasmic loop alone retains a certain function.

Content from these authors
© 2013 THE BIOPHYSICAL SOCIETY OF JAPAN
Previous article Next article
feedback
Top