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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

21.1K
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...
21.1K
Stringent Response in E. coli01:23

Stringent Response in E. coli

494
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
494
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

737
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...
737
Coordination of Gene Expression Processes in Bacteria01:29

Coordination of Gene Expression Processes in Bacteria

1.0K
The DNA replication, transcription, and translation processes are intricately coupled in bacteria, allowing efficient gene expression and rapid protein synthesis. While this physical and functional coordination is advantageous, it introduces challenges that bacteria overcome through specific regulatory mechanisms.Coupling of Replication, Transcription, and TranslationThe coupling of replication, transcription, and translation is a hallmark of bacterial gene expression. As the replisome unwinds...
1.0K

You might also read

Related Articles

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

Sort by
Same author

Efficacy and safety of a novel oral anti-vasculogenic mimicry agent, CVM-1118, in advanced well-differentiated neuroendocrine tumors: a Phase IIa trial.

British journal of cancer·2026
Same author

Response to comment on "Considering the unmeasured impact of 5-fluorouracil dose intensity in the interpretation of optimal initial relative dose intensity of modified FOLFIRINOX".

Journal of the Formosan Medical Association = Taiwan yi zhi·2026
Same author

The Value of Progression-Free Survival in the Perspective of Patients with Multiple Myeloma and Treating Physicians: Research Findings from the US, EU4, UK, Brazil, and Japan.

Clinical lymphoma, myeloma & leukemia·2026
Same author

Response to Comment on "Optimal initial relative dose intensity of modified FOLFIRINOX in pancreatic ductal adenocarcinoma: A retrospective multi-center cohort".

Journal of the Formosan Medical Association = Taiwan yi zhi·2026
Same author

Optimal initial relative dose intensity of modified FOLFIRINOX in pancreatic ductal adenocarcinoma: A retrospective multi-center cohort.

Journal of the Formosan Medical Association = Taiwan yi zhi·2026
Same author

Gemcitabine/nab-paclitaxel plus S-1 combination compared with gemcitabine/nab-paclitaxel in advanced pancreatic ductal adenocarcinoma: a retrospective study.

Therapeutic advances in medical oncology·2026

Related Experiment Video

Updated: Apr 20, 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

4.4K

Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.

Shannon M Doyle1, Shankar Shastry1, Andrea N Kravats1

  • 1Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.

Journal of Molecular Biology
|December 3, 2014
PubMed
Summary

The DnaK/Hsp70 and ClpB/Hsp104 chaperone systems work together to break down protein clumps. Specific interactions within DnaK

Keywords:
GrpEHsp40molecular chaperonenucleotide exchange factorprotein disaggregation

More Related Videos

The Multifaceted Benefits of Protein Co-expression in Escherichia coli
12:48

The Multifaceted Benefits of Protein Co-expression in Escherichia coli

Published on: February 5, 2015

12.6K
Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
07:14

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections

Published on: March 8, 2024

2.1K

Related Experiment Videos

Last Updated: Apr 20, 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

4.4K
The Multifaceted Benefits of Protein Co-expression in Escherichia coli
12:48

The Multifaceted Benefits of Protein Co-expression in Escherichia coli

Published on: February 5, 2015

12.6K
Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
07:14

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections

Published on: March 8, 2024

2.1K

Area of Science:

  • Molecular Biology
  • Protein Homeostasis
  • Chaperone Proteins

Background:

  • The DnaK/Hsp70 chaperone system and ClpB/Hsp104 are essential for disaggregating protein aggregates and reactivating proteins.
  • Specific interactions exist between homologous chaperone pairs, such as E. coli DnaK with E. coli ClpB and yeast Ssa1 with yeast Hsp104.

Purpose of the Study:

  • To identify the specific interaction site on E. coli DnaK that binds to ClpB.
  • To elucidate the molecular mechanism underlying the collaborative function of DnaK/Hsp70 and ClpB/Hsp104 systems in protein disaggregation.

Main Methods:

  • Amino acid substitutions in the DnaK nucleotide-binding domain (NBD), specifically subdomains IB and IIB.
  • Bacterial two-hybrid assays and in vitro fluorescence anisotropy assays to assess DnaK-ClpB interaction.
  • In vitro assays to evaluate the disaggregation and reactivation capabilities of DnaK mutants with ClpB, DnaJ, and GrpE.
  • Computational modeling of the DnaK-ClpB hexamer complex.

Main Results:

  • Mutations in DnaK's NBD subdomains IB and IIB impaired its interaction with ClpB.
  • DnaK subdomain IIB mutants showed defects in protein aggregate disaggregation with ClpB, DnaJ, and GrpE.
  • GrpE competed with ClpB for binding to DnaK, suggesting a common interaction site.
  • Computational modeling indicated that DnaK monomers interact with adjacent ClpB protomers.
  • Homologous mutations in yeast Ssa1 also disrupted Ssa1-Hsp104 collaboration.

Conclusions:

  • Subdomains IB and IIB of the DnaK/Hsp70 NBD are critical for interaction with ClpB/Hsp104.
  • A common and mutually exclusive binding region for GrpE and ClpB exists on DnaK.
  • The findings provide molecular insights into the mechanism of chaperone collaboration for protein disaggregation.
  • The study highlights conserved mechanisms of chaperone cooperation across species.