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Coevolution-Guided Mapping of the Type VI Secretion Membrane Complex-Baseplate Interface.

Etienne Vanlioğlu1, Yoann G Santin1, Isaac Filella-Merce2

  • 1Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), CNRS - Aix-Marseille Université UMR7255, 31 Chemin Joseph Aiguier CS70071, 13402 Marseille Cedex 20, France.

Journal of Molecular Biology
|December 12, 2022
PubMed
Summary
This summary is machine-generated.

Researchers investigated the Type VI secretion system (T6SS) in bacteria, focusing on the TssK-TssL interaction crucial for baseplate-membrane complex assembly. This study proposes a model for this vital interface, enhancing our understanding of bacterial weapon function.

Keywords:
bacterial competitioncoevolutioncontact sitesprotein transportprotein-protein interaction

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • The Type VI secretion system (T6SS) is a complex molecular machine used by Gram-negative bacteria for inter-bacterial or host cell interactions.
  • T6SS function relies on a contractile tail mechanism, with the baseplate and membrane complex forming a critical anchor.
  • Interactions between the TssK baseplate protein and TssL membrane protein are essential for T6SS assembly, but their structural basis remains unclear.

Purpose of the Study:

  • To elucidate the structural basis of the TssK-TssL interaction within the T6SS baseplate-membrane complex.
  • To investigate the functional consequences of disrupting the TssK-TssL interface on T6SS activity and assembly.
  • To develop a model for the TssK-TssL interface using experimental data.

Main Methods:

  • Co-evolution analysis to predict TssK-TssL contact residues.
  • Site-directed mutagenesis of predicted contact pairs in enteroaggregative Escherichia coli.
  • Assessment of T6SS activity, TssK-TssL complex stability, and sheath assembly dynamics.
  • Disulfide cross-linking to probe the TssK-TssL interface.

Main Results:

  • Mutagenesis studies identified key residues mediating the TssK-TssL interaction.
  • Disruptions in the TssK-TssL interface significantly impacted T6SS activity and sheath assembly.
  • Disulfide cross-linking provided evidence for specific contacts within the TssK-TssL interface.
  • A structural model for the baseplate-membrane complex interface was proposed.

Conclusions:

  • The TssK-TssL interaction is critical for the stable assembly and function of the T6SS baseplate-membrane complex.
  • The study provides novel insights into the molecular mechanisms governing T6SS anchoring.
  • The proposed model serves as a foundation for future structural and functional studies of the T6SS.