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Related Concept Videos

Gram-negative Bacterial Protein Secretion Systems01:17

Gram-negative Bacterial Protein Secretion Systems

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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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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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Related Experiment Video

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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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Effector loading onto the VgrG carrier activates type VI secretion system assembly.

Chih-Feng Wu1,2, Yun-Wei Lien1,3,4, Devanand Bondage1

  • 1Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan.

EMBO Reports
|December 7, 2019
PubMed
Summary

Bacterial type VI secretion systems (T6SS) require effector loading for assembly and firing. This ensures toxin delivery and efficient interbacterial competition in Agrobacterium tumefaciens.

Keywords:
Agrobacterium tumefaciensVgrGeffectorinterbacterial competitiontype VI secretion system

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • The type VI secretion system (T6SS) is crucial for bacterial social interactions and host-pathogen dynamics.
  • T6SS regulation is vital due to the high energetic cost of its activity, yet mechanisms remain poorly understood.
  • Agrobacterium tumefaciens utilizes T6SS with Tde DNase toxins for interbacterial competition.

Purpose of the Study:

  • To investigate the role of effectors in the regulation of T6SS assembly and secretion.
  • To elucidate the mechanism linking effector loading to T6SS assembly and function in Agrobacterium tumefaciens.

Main Methods:

  • Investigated T6SS assembly and effector loading in Agrobacterium tumefaciens C58.
  • Utilized genetic analysis to assess the requirement of Tde effectors for TssBC sheath assembly and T6SS secretion.
  • Validated findings across multiple Agrobacterium tumefaciens strains.

Main Results:

  • Tde effector loading onto VgrG spikes is essential for active T6SS secretion.
  • Assembly of the TssBC contractile sheath is dependent on the presence of Tde effectors.
  • This effector-dependent assembly mechanism was confirmed in other Agrobacterium tumefaciens strains.

Conclusions:

  • Bacterial T6SS assembly is regulated by effector loading, ensuring functional secretion.
  • This mechanism guarantees that effectors are loaded before T6SS assembly completion, optimizing firing efficacy.
  • The findings provide new insights into the intricate regulation of bacterial secretion systems.