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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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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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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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Exocrine glands are those that release their secretions through ducts. Based on their mode of secretion, they can be classified into merocrine, apocrine, and holocrine.
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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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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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A Visual Assay to Monitor T6SS-mediated Bacterial Competition
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Mycobacterial type VII secretion systems.

Nikolaos Famelis1, Sebastian Geibel2, Daan van Tol2

  • 1Institute for Molecular Infection Biology, Julius Maximilian University of Würzburg, D-97080 Würzburg, Germany.

Biological Chemistry
|June 5, 2023
PubMed
Summary

Mycobacteria use type VII secretion systems for protein transport. New models integrating structural data and substrate co-dependencies provide a clearer understanding of this complex bacterial secretion pathway.

Keywords:
ESXT7SSpe-ppetranslocasetuberculosis

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Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • Mycobacteria, including M. tuberculosis, employ multiple type VII secretion systems.
  • Protein transport across the mycobacterial cell envelope is complex due to substrate co-dependencies.
  • The precise mechanisms of these secretion systems remain incompletely understood.

Purpose of the Study:

  • To develop detailed and testable models for protein secretion in mycobacteria.
  • To elucidate the role of substrate co-dependencies in type VII secretion.
  • To advance the structural understanding of the secretion machinery.

Main Methods:

  • Structural characterization of inner-membrane secretion machineries.
  • Analysis of substrate co-dependencies for protein transport.
  • Development of mechanistic models for secretion pathways.

Main Results:

  • Detailed models for protein transport via type VII secretion systems have been proposed.
  • The co-dependent nature of substrates significantly influences secretion efficiency.
  • Structural insights into the secretion apparatus provide a foundation for mechanistic understanding.

Conclusions:

  • The study provides a more comprehensive understanding of mycobacterial protein secretion.
  • The developed models offer testable hypotheses for future research.
  • Advances in structural biology and substrate analysis are key to deciphering complex secretion pathways.