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Related Concept Videos

Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

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...
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

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 virus that...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Related Experiment Video

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Screening Foodstuffs for Class 1 Integrons and Gene Cassettes
09:37

Screening Foodstuffs for Class 1 Integrons and Gene Cassettes

Published on: June 19, 2015

Cellular pathways controlling integron cassette site folding.

Céline Loot1, David Bikard, Anna Rachlin

  • 1Institut Pasteur, Unité Plasticité du Génome Bactérien, Paris, France.

The EMBO Journal
|July 15, 2010
PubMed
Summary
This summary is machine-generated.

Integrons facilitate antibiotic resistance spread by mobilizing DNA. Cellular processes and DNA supercoiling influence attC site folding and recombination, regulating integron activity.

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Area of Science:

  • Bacteriology
  • Molecular Biology
  • Genetics

Background:

  • Integrons are key genetic elements driving antibiotic resistance dissemination in bacteria.
  • Gene cassette acquisition by integrons involves recombination between attI and attC sites, catalyzed by IntI1 integrase.
  • This recombination mechanism is unconventional, requiring a folded single-stranded attC site.

Purpose of the Study:

  • To investigate the cellular processes that promote attC site folding.
  • To explore the mechanism of attC site recombination, including extrusion from double-stranded DNA.
  • To determine the influence of DNA superhelicity on attC site extrusion and recombination.

Main Methods:

  • Development of a sensitive in vivo assay to study attC site recombination.
  • In vitro and in vivo experiments to assess the impact of cellular processes and DNA superhelicity.
  • Analysis of attC site folding based on non-recombinogenic structures and variable terminal structures.

Main Results:

  • Bacterial processes like conjugation and replication favor proper attC site folding.
  • attC sites can recombine as cruciform structures extruded from double-stranded DNA.
  • DNA superhelicity influences attC site extrusion both in vitro and in vivo.
  • Proper attC site folding depends on non-recombinogenic structure propensity and terminal structure length.

Conclusions:

  • Cellular processes and DNA superhelicity are critical regulators of integron recombination.
  • Understanding these mechanisms provides insight into the network controlling integron activity and antibiotic resistance spread.