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Understanding Bacterial Flagella Structure and Function
Sep 20, 2024
Bacterial Flagella and Their Function
Overview
Bacterial flagella are motorized structures that bacteria use to propel themselves.
Rotobacter
: Single flagellum.
E. coli
: Multiple flagella that rotate in bundles.
Flagellum characteristics:
Helical filament: 20nm wide, up to 15 microns long.
Spin rate: ~100 times per second.
Structure of the Flagellum
Three main parts:
Filament
: The long, helical structure visible outside the cell.
Hook
: Flexible connector between the filament and the basal body.
Basal body
: Anchors the flagellum to the cell wall; comprises a rod and rings:
Inner membrane rings
Peptidoglycan layer rings
Outer membrane rings (L and P rings in gram-negative bacteria)
Flagellar Motor
Composed of the
stator
and
rotor
:
Stator
: Stationary; attached to the peptidoglycan layer.
Rotor
: Rotational component.
Power source
: Proton gradient across the cell membrane.
High proton concentration outside; low inside.
Proton flow
: Through proteins
MOTA
and
MOTB
in the stator.
Mechanism of Action
MOTB
contains aspartic acid crucial for proton conductance.
Proton movement
: Binding to aspartic acid causes conformational changes in MOTA.
Results in two consecutive power strokes driving the rotor.
Protons are released into the cytoplasm.
Assembly of Flagella
Begins with structures in the inner membrane:
MS ring
: Formed by 26 subunits of Flea F protein.
Flea G, M, and N
: Assemble under the MS ring, constitute the rotor.
Extracellular assembly
:
Flagellar proteins exported via a specific export pathway.
Mote A and Mote B
: Form the stator, anchoring in the peptidoglycan layer.
Rod assembly
: Built upward through a hollow cylinder, guided by cap proteins.
Outer membrane penetration
:
L and P rings
: Serve as bearings for the rod.
Hook and Filament assembly
:
Hook cap guides hook protein assembly.
Junction proteins connect hook and filament.
Filament proteins travel through a hollow channel to the distal end, building helically.
Filament structure
: 20,000 to 30,000 subunits.
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