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Gram-negative bacteria utilize sophisticated protein secretion systems to transport proteins across their double-membrane envelope into the extracellular environment or host cells. Based on their mechanism of action, these systems are classified into one-step and two-step pathways.One-Step Secretion Systems (Types I, III, IV, and VI)One-step secretion systems bypass the periplasm entirely, forming a continuous channel that spans both the inner and outer membranes:Type I Secretion System (T1SS):...
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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Related Experiment Video

Updated: Apr 16, 2026

A Visual Assay to Monitor T6SS-mediated Bacterial Competition
08:45

A Visual Assay to Monitor T6SS-mediated Bacterial Competition

Published on: March 20, 2013

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Atomic structure of T6SS reveals interlaced array essential to function.

Daniel L Clemens1, Peng Ge2, Bai-Yu Lee1

  • 1Department of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Cell
|February 28, 2015
PubMed
Summary
This summary is machine-generated.

Researchers identified the Type VI secretion system (T6SS) in Francisella, revealing its structure and function. This discovery aids in developing drugs targeting this bacterial secretion apparatus.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Bacterial Pathogenesis

Background:

  • Type VI secretion systems (T6SSs) are bacterial nanomachines for protein translocation.
  • The Francisella pathogenicity island was suspected to encode a T6SS-like apparatus crucial for virulence.

Purpose of the Study:

  • To confirm the presence and characterize the structure of the T6SS in Francisella.
  • To elucidate the role of the T6SS structure in bacterial function and pathogenesis.

Main Methods:

  • Cryo-electron microscopy (cryoEM) was used to determine the structure of the TSS6 post-contraction sheath.
  • Structure-based mutagenesis was employed to investigate functional significance.
  • Assembly and secretion assays were performed.

Main Results:

  • The T6SS apparatus in Francisella was experimentally confirmed.
  • The cryoEM structure of the post-contraction sheath was resolved at 3.7 Å resolution.
  • The sheath exhibits a unique interlaced 2D array structure essential for secretion, phagosomal escape, and replication.

Conclusions:

  • The characterized T6SS is vital for Francisella virulence, mediating phagosomal escape and intracellular replication.
  • The unique structural features, particularly the interlaced sheath, are critical for T6SS function.
  • The atomic model provides a basis for designing targeted therapeutics against this prevalent secretion system.