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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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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Protein Translocation Machinery on the ER Membrane01:28

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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Bacterial Translocation and Protein Secretion01:26

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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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Coat Assembly and GTPases01:33

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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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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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Structural Model of a Porphyromonas gingivalis type IX Secretion System Shuttle Complex.

Ben Dorgan1, Yichao Liu2, Sunjun Wang2

  • 1Centre for Host-Microbiome Interactions, Faculty of Dental, Oral & Craniofacial Sciences, King's College London, London, UK; School of Biological and Chemical Sciences, Queen Mary University of London, London, UK.

Journal of Molecular Biology
|November 21, 2022
PubMed
Summary
This summary is machine-generated.

Porphyromonas gingivalis uses the type IX secretion system (T9SS) to export virulence factors like RgpB. Researchers structurally modeled the interaction between PorV and RgpB

Keywords:
CTDPorVPorphyromonas gingivalisRgpBT9SS

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Porphyromonas gingivalis is a key pathogen in periodontitis.
  • Virulence factors are exported via the type IX secretion system (T9SS).
  • Cargo proteins require a C-terminal domain (CTD) for T9SS recognition.

Purpose of the Study:

  • To elucidate the structural mechanism of CTD recognition by the T9SS.
  • To present a structural model of the PorV:RgpB-CTD complex.

Main Methods:

  • Solution nuclear magnetic resonance (NMR) spectroscopy
  • Biochemical analyses
  • Machine-learning-based modeling
  • Molecular dynamics (MD) simulations

Main Results:

  • A structural model of the PorV:RgpB-CTD complex was determined.
  • Conserved motifs in the CTD are critical for binding to PorV.
  • Extracellular loops of PorV mediate CTD binding, cradling the cargo.

Conclusions:

  • This study provides the first structural insight into CTD recognition by the T9SS.
  • Understanding PorV-CTD interaction is crucial for P. gingivalis pathogenesis.
  • Findings may inform broader understanding of type IX secretion.