Priming and polymerization of a bacterial contractile tail structure

Nature. 2016 Mar 3;531(7592):59-63. doi: 10.1038/nature17182. Epub 2016 Feb 24.


Contractile tails are composed of an inner tube wrapped by an outer sheath assembled in an extended, metastable conformation that stores mechanical energy necessary for its contraction. Contraction is used to propel the rigid inner tube towards target cells for DNA or toxin delivery. Although recent studies have revealed the structure of the contractile sheath of the type VI secretion system, the mechanisms by which its polymerization is controlled and coordinated with the assembly of the inner tube remain unknown. Here we show that the starfish-like TssA dodecameric complex interacts with tube and sheath components. Fluorescence microscopy experiments in enteroaggregative Escherichia coli reveal that TssA binds first to the type VI secretion system membrane core complex and then initiates tail polymerization. TssA remains at the tip of the growing structure and incorporates new tube and sheath blocks. On the basis of these results, we propose that TssA primes and coordinates tail tube and sheath biogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Escherichia coli / chemistry*
  • Escherichia coli / ultrastructure
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Escherichia coli Proteins / ultrastructure
  • Microscopy, Electron
  • Microscopy, Fluorescence
  • Models, Molecular
  • Polymerization*
  • Protein Structure, Tertiary
  • Type VI Secretion Systems / chemistry
  • Type VI Secretion Systems / metabolism
  • Type VI Secretion Systems / ultrastructure


  • Escherichia coli Proteins
  • TssA protein, E coli
  • Type VI Secretion Systems

Associated data

  • PDB/4YO3
  • PDB/4YO5