Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Microbial Interactions: Predation01:28

Microbial Interactions: Predation

Microbial predation refers to the process by which one microorganism kills and consumes another to obtain nutrients and energy. It encompasses both bacterial and protozoan predators. This interaction plays a crucial role in shaping microbial communities and regulating nutrient cycling.Bacterial Predators: Epibiotic vs. EndobioticBacterial predators are classified based on their mode of attack as either epibiotic or endobiotic. Epibiotic predators, such as Vampirococcus, attach to the surface of...
Microbial Interactions: Parasitism01:22

Microbial Interactions: Parasitism

Parasitism is a form of microbial interaction in which parasitic microbes exploit a host organism for nutrients and shelter, often at the host's expense. Unlike mutualistic relationships, where both organisms benefit, parasitism benefits only the parasite and harms the host.Classification of ParasitesMicrobial parasites are broadly classified based on their location relative to the host.Ectoparasites remain on the host’s surface, such as the skin or outer tissues, drawing nutrients...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Interactions between non-prion and prion domains of Rnq1 direct formation of amyloid vs liquid-like aggregates and create transmission barriers.

bioRxiv : the preprint server for biology·2026
Same author

Deletion of the Saccharomyces cerevisiae RACK1 homolog, ASC1, enhances autophagy which mitigates TDP-43 toxicity.

Genetics·2026
Same author

Deletion of the <i>Saccharomyces cerevisiae RACK1</i> homolog, <i>ASC1</i> , enhances autophagy which mitigates TDP-43 toxicity.

bioRxiv : the preprint server for biology·2025
Same author

An adenine model of inborn metabolism errors alters TDP-43 aggregation and reduces its toxicity in yeast revealing insights into protein misfolding diseases.

Microbial cell (Graz, Austria)·2025
Same author

A model of inborn metabolism errors associated with adenine amyloid-like fiber formation reduces TDP-43 aggregation and toxicity in yeast.

bioRxiv : the preprint server for biology·2024
Same author

Expression of Wild-Type and Mutant Human TDP-43 in Yeast Inhibits TOROID (TORC1 Organized in Inhibited Domain) Formation and Autophagy Proportionally to the Levels of TDP-43 Toxicity.

International journal of molecular sciences·2024
Same journal

Correction.

Prion·2026
Same journal

Early diagnosis of a case of Heidenhain variant of Creutzfeld-Jakob disease by cerebrospinal fluid real-time quaking-induced conversion test.

Prion·2026
Same journal

In memoriam of Pawel P. Liberski (1954-2025).

Prion·2026
Same journal

Maternal chronic wasting disease infection restricts fetal head size in white-tailed deer (<i>Odocoileus virginianus</i>).

Prion·2026
Same journal

Plaque-type dura mater graft-associated Creutzfeldt-Jakob disease: an autopsied case report.

Prion·2026
Same journal

Efficient induction of motor neuron disease in transgenic G93A SOD1 mice by prion-like seeding.

Prion·2026
See all related articles

Related Experiment Video

Updated: Jun 26, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Prion-prion interactions.

Irina L Derkatch1, Susan W Liebman

  • 1Department of Microbiology, New York University School of Medicine, New York University Medical Center, New York, New York 10016, USA. irina.derkatch@med.nyu.edu

Prion
|January 24, 2009
PubMed
Summary
This summary is machine-generated.

Prions, self-replicating protein conformations, influence each other's formation and spread in yeast. These interactions, including cross-seeding, can be direct or mediated by cellular factors, affecting prion propagation.

More Related Videos

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Related Experiment Videos

Last Updated: Jun 26, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Prions are self-replicating protein conformations capable of converting native proteins into the prion form.
  • Several proteins in Saccharomyces cerevisiae (yeast) have been identified as prions.
  • Interactions between different prion proteins in the same cell are complex and can influence their propagation.

Purpose of the Study:

  • To investigate the influence of heterologous prions on each other's appearance and propagation in Saccharomyces cerevisiae.
  • To elucidate the mechanisms underlying prion-prion interactions, including direct protein-protein interactions and cellular factor involvement.

Main Methods:

  • Genetic studies in Saccharomyces cerevisiae to observe prion interactions in vivo.
  • In vitro experiments using purified prion proteins to study direct conversion mechanisms.
  • Analysis of cellular factors, such as the cytoskeleton and chaperones, potentially mediating prion interactions.

Main Results:

  • Heterologous prion proteins significantly influence each other's de novo appearance and propagation.
  • Observed interactions include both positive effects (facilitation) and negative effects (inhibition, destabilization).
  • In vitro studies suggest direct cross-seeding interactions between purified prions, independent of other cellular components.

Conclusions:

  • Prion-prion interactions in yeast are multifaceted, involving direct protein interactions (cross-seeding) and modulation by cellular components like chaperones and the cytoskeleton.
  • These interactions can either promote or inhibit prion formation and propagation, highlighting the complexity of prion biology.
  • Understanding these interactions is crucial for comprehending prion propagation mechanisms in vivo.