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TitlePriming and polymerization of a bacterial contractile tail structure.
Journal, issue, pagesNature, Vol. 531, Issue 7592, Page 59-63, Year 2016
Publish dateMar 3, 2016
AuthorsAbdelrahim Zoued / Eric Durand / Yannick R Brunet / Silvia Spinelli / Badreddine Douzi / Mathilde Guzzo / Nicolas Flaugnatti / Pierre Legrand / Laure Journet / Rémi Fronzes / Tâm Mignot / Christian Cambillau / Eric Cascales /
PubMed AbstractContractile 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 ...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.
External linksNature / PubMed:26909579
MethodsEM (single particle) / X-ray diffraction
Resolution3.35 - 19.0 Å
Structure data

EMDB-3282:
Negative stain electron microscopy structure of TssA from EAEC type VI secretion system
Method: EM (single particle) / Resolution: 19.0 Å

PDB-4yo3:
Enteroaggregative Escherichia Coli TssA N-terminal fragment
Method: X-RAY DIFFRACTION / Resolution: 3.37 Å

PDB-4yo5:
EAEC T6SS TssA-Cterminus
Method: X-RAY DIFFRACTION / Resolution: 3.35 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • escherichia coli 042 (bacteria)
KeywordsTRANSPORT PROTEIN / Type VI secretion system / TssA

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