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Cytoskeletal Proteins in Bacteria

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Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
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Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a...
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Visualization of Bacterial Toxin Induced Responses Using Live Cell Fluorescence Microscopy
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Revisiting bacterial cytolethal distending toxin structure and function.

Henry Chen1, Claire J Ang1, Molly K Crowder1

  • 1Department of Microbiology, School of Molecular and Cellular Biology, University of Illinois at Urbana-Champaign, Urbana, IL, United States.

Frontiers in Cellular and Infection Microbiology
|November 30, 2023
PubMed
Summary
This summary is machine-generated.

Cytolethal distending toxins (CDTs) require specific subunits for host cell activity. This study shows that functional Campylobacter jejuni CDT (Cj-CDT) does not require preassembled heterotrimers, challenging existing models.

Keywords:
AB toxinCampylobacter jejuniDNA damagecytolethal distending toxinholotoxin structureprotein-protein interactions

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Toxicology

Background:

  • Cytolethal distending toxins (CDTs) are bacterial genotoxins produced by pathogens.
  • CDTs target host cells by binding to the plasma membrane.
  • Maximal CDT activity is thought to require a preassembled tripartite complex of CdtA, CdtB, and CdtC subunits.

Purpose of the Study:

  • To experimentally investigate the relationship between subunit interactions and cellular activity of Campylobacter jejuni CDT (Cj-CDT).
  • To determine if preassembled heterotrimeric complexes are necessary for Cj-CDT's genotoxic effects.

Main Methods:

  • Co-immunoprecipitation and dialysis retention assays to detect heterotrimeric complexes.
  • Microscale thermophoresis to assess subunit interaction affinity.
  • Cell cycle arrest assays to measure toxin activity at the G2/M interface.

Main Results:

  • Heterotrimeric Cj-CDT complexes were detected only at very high subunit concentrations.
  • Low affinity interactions were observed between Cj-CDT subunits.
  • Toxin-mediated cell cycle arrest occurred at subunit concentrations significantly lower than those forming heterotrimers.

Conclusions:

  • The widely accepted model of CDTs acting as preassembled heterotrimers is challenged by these findings.
  • At effective concentrations, Cj-CDT likely functions as a mixture of non-interacting subunits.
  • Further research is needed to elucidate the precise mechanism of CDT intoxication.