Contribution to the elucidation of the structure of the bacterial flagellum nano-motor through AFM imaging of the M-Ring.
The flagellar nano-motor of bacteria is one of the most interesting and amazing natural nano-machine. Despite its discovery 30 years ago, some details of its structure and mechanisms are not yet elucidated. Several studies have revealed some important aspects of its structure and numerous data are available today; however, the inner mechanisms of the nano-motor have not been yet resolved, partially due to the lack of information about the 3D assembly, shape and interactions of the different parts in experimental environment as close as possible as the native cellular conditions. We have developed an approach using atomic force microscopy imaging in liquid media, which allows us to study part of the motor in native liquid environment. In this work, we are interested in the FliG proteins, identified as the key functional proteins of this nano-machine. We report 3D images of their assembly on surfaces, which could be representative of the so-called M-ring part of the nano-motor. These images have been acquired on both mica surfaces and on supported bilayer membranes mimetics of E. coli native membrane. The systematic analysis of the shape and the size of different recorded assemblies made us believe that the FliG organization we observed could lead to a new model for the structure and mechanism of the flagellar nano-motor.
Chalmeau
Jerome
J
LAAS-CNRS, Université de Toulouse, 7 Avenue du Colonel Roche, F-31077 Toulouse, France. jchalmea@laas.fr
Dagkessamanskaia
Adilia
A
Le Grimellec
Christian
C
Francois
Jean-marie
JM
Sternick
John
J
Vieu
Christophe
C
D001426:Bacterial Proteins / Q000378:metabolism / Q000648:ultrastructure*; D002462:Cell Membrane / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000648:ultrastructure*; D005407:Flagella / Q000648:ultrastructure*; D007091:Image Processing, Computer-Assisted / Q000379:methods; D046911:Macromolecular Substances; D018625:Microscopy, Atomic Force / Q000379:methods*; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000378:metabolism / Q000648:ultrastructure*; D011485:Protein Binding
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C075660:Flig protein, Bacteria; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins