期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 38, 页码 27031-27041出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.499772
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资金
- Centre National de la Recherche Scientifique (CNRS)
- Aix-Marseille University
- Agence Nationale de la Recherche [ANR-10-JCJC-1303-03]
- CNRS
- Marseille-Nice Genopole
- IBiSA
- Fondation de la Recherche Medicale [FRM DEQ2011-0421282]
- French Ministere de la Recherche
- Fondation pour la Recherche Medicale [SPF20101221116]
The Type VI secretion system (T6SS) is a macromolecular machine that mediates bacteria-host or bacteria-bacteria interactions. The T6SS core apparatus assembles from 13 proteins that form two sub-assemblies: a phage-like complex and a trans-envelope complex. The Hcp, VgrG, TssE, and TssB/C subunits are structurally and functionally related to components of the tail of contractile bacteriophages. This phage-like structure is thought to be anchored to the membrane by a trans-envelope complex composed of the TssJ, TssL, and TssM proteins. However, how the two sub-complexes are connected remains unknown. Here we identify TssK, a protein that establishes contacts with the two T6SS sub-complexes through direct interactions with TssL, Hcp, and TssC. TssK is a cytoplasmic protein assembling trimers that display a three-armed shape, as revealed by TEM and SAXS analyses. Fluorescence microscopy experiments further demonstrate the requirement of TssK for sheath assembly. Our results suggest a central role for TssK by linking both complexes during T6SS assembly.
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