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Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor
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Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor
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Journal Article
Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor
2016
Overview
A combination of evolutionary covariance, biochemistry and SAXS analyses reveal that
Escherichia coli
FliG exists as a monomer in solution but forms domain-swapped polymers in assembled flagellar motors, thus leading to a thermodynamic model for self-assembly.
Large protein complexes assemble spontaneously, yet their subunits do not prematurely form unwanted aggregates. This paradox is epitomized in the bacterial flagellar motor, a sophisticated rotary motor and sensory switch consisting of hundreds of subunits. Here we demonstrate that
Escherichia coli
FliG, one of the earliest-assembling flagellar motor proteins, forms ordered ring structures via domain-swap polymerization, which in other proteins has been associated with uncontrolled and deleterious protein aggregation. Solution structural data, in combination with
in vivo
biochemical cross-linking experiments and evolutionary covariance analysis, revealed that FliG exists predominantly as a monomer in solution but only as domain-swapped polymers in assembled flagellar motors. We propose a general structural and thermodynamic model for self-assembly, in which a structural template controls assembly and shapes polymer formation into rings.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ 14/34
/ 14/63
/ 38/70
/ 82/16
/ 82/29
/ 82/81
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ E coli
/ Escherichia coli - chemistry
/ Macromolecular Substances - chemistry
/ Macromolecular Substances - metabolism
/ Magnetic Resonance Spectroscopy
/ Molecular Motor Proteins - chemistry
/ Molecular Motor Proteins - metabolism
/ Molecular motors (Biochemistry)
/ Polymers
/ Proteins
