Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1038/nsmb.3172

Type

Journal article

Journal

Nat Struct Mol Biol

Publication Date

03/2016

Volume

23

Pages

197 - 203

Keywords

Bacterial Proteins, Escherichia coli, Flagella, Macromolecular Substances, Magnetic Resonance Spectroscopy, Models, Biological, Models, Chemical, Models, Molecular, Molecular Motor Proteins, Organelle Biogenesis, Protein Conformation, Protein Multimerization