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

13.0K
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,...
13.0K
Amyloid Fibrils03:03

Amyloid Fibrils

7.0K
7.0K
Bacterial Phylum Actinobacteria01:30

Bacterial Phylum Actinobacteria

851
Coryneform bacteria are gram-positive, aerobic, nonmotile rods that exhibit irregular, club-shaped, or V-shaped arrangements. Their V-shape results from snapping division, where the inner cell wall layer forms the cross-wall, while the outer layer remains intact until it ruptures on one side, causing the daughter cells to bend away.The primary genera are Corynebacterium and Arthrobacter. Corynebacterium includes diverse species, ranging from saprophytes to pathogens like Corynebacterium...
851
Amino Acid Catabolism01:18

Amino Acid Catabolism

1.6K
Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
1.6K
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

4.5K
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...
4.5K
Cell Inclusions01:27

Cell Inclusions

1.4K
Prokaryotic cells possess a variety of inclusions that play crucial roles in nutrient storage, metabolic processes, and environmental adaptation. These structures enable bacteria to thrive under fluctuating environmental conditions by storing essential resources and optimizing their metabolic efficiency.Carbon Storage: Poly-β-Hydroxybutyric Acid and Glycogen GranulesBacteria frequently store excess carbon in specialized granules. Poly-β-hydroxybutyric acid (PHB) granules are lipid...
1.4K

You might also read

Related Articles

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

Sort by
Same author

BAMBI: A novel regulator of intestinal epithelial integrity in the control of colitis and colon cancer progression.

Mucosal immunology·2026
Same author

Professional Academies: The Duty to Lead.

Microbial biotechnology·2026
Same author

Early seed priming with closely related <i>Bacillus</i> strains induces divergent physiological and defense responses in melon.

Horticulture research·2026
Same author

Oxytetracycline as an otolith chemical marker in Atlantic bluefin tuna (Thunnus thynnus): Technical feasibility in culture.

Journal of fish biology·2026
Same author

Matrix plasticity and the molecular basis of extracellular filament assembly in <i>Bacillus cereus</i>.

Science advances·2026
Same author

Cadmium, lead and mercury accumulation in European eel (Anguilla anguilla) from four Mediterranean wetlands: Tissue-specific patterns and management implications.

Marine pollution bulletin·2026

Related Experiment Video

Updated: Apr 1, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.6K

Functional amyloids in bacteria.

Diego Romero1, Roberto Kolter2

  • 1Institute of Subtropical and Mediterranean Hortofruticulture "La Mayora"- CSIC, and Department of Microbiology, University of Malaga, Malaga, Spain.

International Microbiology : the Official Journal of the Spanish Society for Microbiology
|September 30, 2015
PubMed
Summary

Amyloidosis involves protein fibers that can be toxic or functional. This review explores beneficial, functional amyloid proteins in bacteria, highlighting their role in cellular homeostasis and surface assembly.

Keywords:
Bacillus subtilisTasA amyloid-like fibersbacterial biofilmsextracellular matrix

More Related Videos

Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa
07:27

Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa

Published on: July 12, 2018

6.0K
Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

3.8K

Related Experiment Videos

Last Updated: Apr 1, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.6K
Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa
07:27

Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa

Published on: July 12, 2018

6.0K
Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

3.8K

Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Amyloidosis is a group of diseases characterized by protein aggregates in human organs.
  • Amyloid fibers, though diverse in sequence, share a common structure rich in beta-sheets, conferring stability and insolubility.
  • These fibers are not exclusively pathogenic and are found across various organisms, including bacteria.

Purpose of the Study:

  • To review bacterial systems that regulate the expression and assembly of amyloid proteins on cell surfaces.
  • To explore the beneficial roles of these "functional amyloids" in microbial homeostasis.
  • To differentiate functional amyloids from their pathogenic counterparts.

Main Methods:

  • Literature review of studies on bacterial amyloid protein systems.
  • Analysis of structural and functional properties of functional amyloids.
  • Examination of regulatory mechanisms for amyloid assembly in bacteria.

Main Results:

  • Amyloid fiber formation is a conserved process with roles beyond human disease.
  • Bacteria utilize amyloid proteins on their surfaces for beneficial functions.
  • Specific systems in bacteria control the controlled expression and assembly of these robust protein structures.

Conclusions:

  • Functional amyloids represent a significant class of protein structures with essential roles in microbial life.
  • Understanding bacterial amyloid systems offers insights into protein assembly and homeostasis.
  • The study of functional amyloids in bacteria provides a model for exploring protein structure-function relationships.