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Related Experiment Videos

The outer membrane usher forms a twin-pore secretion complex.

Huilin Li1, Luping Qian, Zhiqiang Chen

  • 1Biology Department, Brookhaven National Laboratory, 50 Bell Ave, Upton, NY 11973, USA.

Journal of Molecular Biology
|November 25, 2004
PubMed
Summary
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The PapC usher protein in E. coli forms a twin-pore dimer essential for P pilus assembly. Its C-terminal domain influences this dimerization, impacting outer membrane protein secretion.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The PapC usher is crucial for P pilus assembly and secretion in uropathogenic Escherichia coli.
  • P pilus biogenesis utilizes the chaperone/usher pathway, a part of the general secretory pathway.
  • Molecular mechanisms of pilus biogenesis at the usher and outer membrane protein secretion remain unclear.

Purpose of the Study:

  • To investigate the structure and oligomeric state of the PapC usher.
  • To elucidate the role of the C-terminal domain in PapC structure and function.

Main Methods:

  • Gel filtration
  • Dynamic light scattering
  • Electron microscopy and image analysis
  • Two-dimensional crystallization of PapC

Related Experiment Videos

  • Reconstitution into E. coli lipids

    • Main Results:

    • PapC forms a dimer in detergent solution and in phospholipid bilayers.
    • Cryo-electron microscopy revealed PapC as a twin-pore complex.
    • The C-terminal domain is involved in the dimeric association of the PapC usher.

    Conclusions:

    • PapC forms a dimeric twin-pore complex essential for P pilus biogenesis.
    • The C terminus of PapC plays a role in usher dimerization.
    • The structural features of PapC resemble the mitochondrial Tom40 translocase.