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

11.5K
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,...
11.5K
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

4.1K
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...
4.1K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

402
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
402
Protein Complex Assembly02:41

Protein Complex Assembly

16.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.5K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.5K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.5K
Bacterial Phylum Actinobacteria01:30

Bacterial Phylum Actinobacteria

561
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...
561

You might also read

Related Articles

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

Sort by
Same author

Bacillus subtilis DnaB forms multiple protein-protein interactions essential for DNA replication initiation.

Nucleic acids research·2026
Same author

Polyphosphate synthesis is essential for phosphate and ATP homeostasis during nutrient upshift.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Addendum: Widespread potential for phototrophy and convergent reduction of lifecycle complexity in the dimorphic order Caulobacterales.

Nature communications·2026
Same author

Overcoming Cancer Disparities Globally: Contributions of Norman Coleman.

Disaster medicine and public health preparedness·2026
Same author

Widespread potential for phototrophy and convergent reduction of lifecycle complexity in the dimorphic order Caulobacterales.

Nature communications·2025
Same author

Diversity and evolution of alphaproteobacterial dimorphism.

Current opinion in microbiology·2025
Same journal

Feeding the invaders: How metabolic imbalance shapes infection and biofilm development.

FEMS microbiology reviews·2026
Same journal

Interactions between extracellular vesicles and viruses: lessons learned across species and kingdoms.

FEMS microbiology reviews·2026
Same journal

Killer Peptide: an antibody-derived self-assembling peptide bridging antimicrobial and host-defense mechanisms.

FEMS microbiology reviews·2026
Same journal

From gatekeeper to target: MAPK cascades as control circuits at the insect-microbe interface.

FEMS microbiology reviews·2026
Same journal

The role of fungal G protein-coupled receptors in interspecies cell-cell communication.

FEMS microbiology reviews·2026
Same journal

Convergent symbioses: morphology, life history, and niche specialization in coral and lichen mutualisms.

FEMS microbiology reviews·2026
See all related articles

Related Experiment Video

Updated: Jan 5, 2026

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
07:59

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

Published on: June 29, 2021

4.1K

Protein aggregation in bacteria.

Frederic D Schramm1, Kristen Schroeder1, Kristina Jonas1

  • 1Science for Life Laboratory and Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Svante Arrhenius väg 20C, Stockholm 10691, Sweden.

FEMS Microbiology Reviews
|October 22, 2019
PubMed
Summary
This summary is machine-generated.

Bacterial protein aggregation, linked to stress and disease, shows diverse strategies across species. Understanding this process reveals insights into bacterial fitness and evolution.

Keywords:
aggregate inheritancecellular agingdisaggregasesmolecular chaperonesprotein aggregationstress adaptation

More Related Videos

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.8K
Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.6K

Related Experiment Videos

Last Updated: Jan 5, 2026

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
07:59

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

Published on: June 29, 2021

4.1K
4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.8K
Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.6K

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein aggregation arises from disrupted protein homeostasis due to cellular stresses.
  • Accumulated aggregates are linked to aging, pathologies, and altered bacterial traits like virulence and growth.
  • While studied in *E. coli*, bacterial responses to protein aggregation exhibit phylogenetic diversity.

Purpose of the Study:

  • To review recent advances in understanding bacterial protein aggregation.
  • To highlight diverse strategies bacteria use to cope with protein aggregation.
  • To discuss the consequences of protein aggregation on bacterial populations and gene regulation.

Main Methods:

  • Literature review of recent research on bacterial protein aggregation.
  • Comparative analysis of protein quality control machinery across different bacterial phyla.
  • Synthesis of findings on aggregate localization, inheritance, and fitness impacts.

Main Results:

  • Significant diversity exists in how different bacterial species manage protein aggregation.
  • The inheritance and population-level fitness consequences of protein aggregates are still debated.
  • Specific protein aggregates can play regulatory roles in gene expression and resource allocation.

Conclusions:

  • Bacterial protein aggregation is a complex phenomenon with varied implications across the bacterial kingdom.
  • Further research is needed to fully elucidate the mechanisms and consequences of protein aggregation in diverse bacteria.
  • Protein aggregation is not solely a detrimental stress response but can also be a regulatory mechanism.