Type VI secretion and bacteriophage tail tubes share a common assembly pathway
| Autor: | Eric Cascales, Yannick R. Brunet, Herve Celia, Jérôme Hénin |
|---|---|
| Přispěvatelé: | Laboratoire d'ingénierie des systèmes macromoléculaires (LISM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU), Laboratoire de biochimie théorique [Paris] (LBT (UPR_9080)), Institut de biologie physico-chimique (IBPC (FR_550)), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Virulence Factors
[SDV]Life Sciences [q-bio] Molecular Sequence Data Stacking Plasma protein binding Biology Biochemistry Bacteriophage Escherichia coli Genetics [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Secretion Amino Acid Sequence Bacterial Secretion Systems Molecular Biology Peptide sequence ComputingMilieux_MISCELLANEOUS Type VI secretion system Effector Escherichia coli Proteins Scientific Reports biology.organism_classification Protein Structure Tertiary Biophysics Protein Multimerization Protein Binding Macromolecule |
| Zdroj: | EMBO Reports EMBO Reports, EMBO Press, 2014, 15 (3), pp.315-321. ⟨10.1002/embr.201337936⟩ EMBO Reports, 2014, 15 (3), pp.315--21. ⟨10.1002/embr.201337936⟩ EMBO Reports, 2014, 15 (3), pp.315-321. ⟨10.1002/embr.201337936⟩ EMBO Reports, EMBO Press, 2014, 15 (3), pp.315--21. ⟨10.1002/embr.201337936⟩ |
| ISSN: | 1469-221X 1469-3178 |
| DOI: | 10.1002/embr.201337936⟩ |
| Popis: | International audience; The Type VI secretion system (T6SS) is a widespread macromolecular structure that delivers protein effectors to both eukaryotic and prokaryotic recipient cells. The current model describes the T6SS as an inverted phage tail composed of a sheath-like structure wrapped around a tube assembled by stacked Hcp hexamers. Although recent progress has been made to understand T6SS sheath assembly and dynamics, there is no evidence that Hcp forms tubes in vivo. Here we show that Hcp interacts with TssB, a component of the T6SS sheath. Using a cysteine substitution approach, we demonstrate that Hcp hexamers assemble tubes in an ordered manner with a head-to-tail stacking that are used as a scaffold for polymerization of the TssB/C sheath-like structure. Finally, we show that VgrG but not TssB/C controls the proper assembly of the Hcp tubular structure. These results highlight the conservation in the assembly mechanisms between the T6SS and the bacteriophage tail tube/sheath. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text