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Stochastic chain termination in bacterial pilus assembly.

Christoph Giese1, Chasper Puorger2,3, Oleksandr Ignatov2,4

  • 1Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, 8093, Zurich, Switzerland. giesec@mol.biol.ethz.ch.

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Uropathogenic E. coli type 1 pili assembly is terminated by subunit FimI, creating a stochastic chain reaction that dictates pilus length. FimI also anchors pili to the outer membrane.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Type 1 pili are essential virulence factors in uropathogenic Escherichia coli.
  • Pili are filamentous protein structures assembled via the chaperone-usher pathway.
  • The precise regulation of pilus length is not fully understood.

Purpose of the Study:

  • To elucidate the mechanism of type 1 pilus rod assembly and length regulation.
  • To identify the subunit responsible for assembly termination.
  • To determine the structural basis of pilus assembly and anchoring.

Main Methods:

  • In vitro reconstitution of type 1 pilus rod assembly.
  • Quantitative kinetic modeling of subunit incorporation.
  • Crystal structure determination of key protein complexes.
  • Analysis of pilus length distribution in vitro and in vivo.

Main Results:

  • FimI was identified as an irreversible assembly terminator for type 1 pili.
  • A quantitative model accurately predicts pilus rod length distribution based on FimI/FimA ratio.
  • FimI plays a role in anchoring pili to the outer membrane.
  • Crystal structures provide insights into assembly termination and FimI function.

Conclusions:

  • Pilus length is regulated by a stochastic chain termination reaction involving FimI.
  • FimI is a crucial component for both pilus length control and outer membrane anchoring.
  • Structural data reveals the molecular mechanisms underlying type 1 pilus assembly regulation.