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 Experiment Videos

Molecular chaperones: clamps for the Clps?

H P Feng1, L M Gierasch

  • 1Department of Chemistry, University of Massachusetts, Amherst 01003, USA.

Current Biology : CB
|July 4, 1998
PubMed
Summary

Clp/Hsp100 molecular chaperones can untangle protein clumps and complexes. These chaperones likely use PDZ-like domains to bind substrates, a strategy for controlling protein assembly states.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Corrigendum to "Mutations and clinical significance of calcium voltage-gated channel subunit alpha 1E (CACNA1E) in non-small cell lung cancer" [Cell Calcium 102 (2022) 102527].

Cell calcium·2024
Same author

[Clinical features and related factors of invasive pulmonary aspergillosis in patients with acute exacerbation of chronic obstructive pulmonary disease].

Zhonghua yi xue za zhi·2023
Same author

Peptides and the development of double- and triple-resonance solid-state NMR of aligned samples.

The journal of peptide research : official journal of the American Peptide Society·2005
Same author

Defining the structure of the substrate-free state of the DnaK molecular chaperone.

Biochemical Society symposium·2001
Same author

The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle.

The Journal of biological chemistry·2001
Same author

Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity.

The Journal of biological chemistry·2001

Area of Science:

  • Protein biochemistry
  • Molecular biology
  • Cellular machinery

Background:

  • Clp/Hsp100 proteins are molecular chaperones known for their unique ability to dismantle protein aggregates and complexes.
  • Understanding the substrate binding mechanism of these chaperones is crucial for deciphering their function in protein quality control.

Purpose of the Study:

  • To investigate the mechanism by which Clp/Hsp100 molecular chaperones interact with and manipulate their substrate proteins.
  • To explore the potential role of PDZ-like domains in substrate recognition and binding by Clp/Hsp100 chaperones.

Main Methods:

  • Analysis of protein-protein interactions.
  • Biochemical assays to study chaperone activity.
  • Structural biology techniques to investigate domain interactions.

Main Results:

  • Evidence suggests that Clp/Hsp100 chaperones bind substrates through PDZ-like domains.
  • This binding mechanism appears to be a key factor in the chaperone's ability to resolve protein aggregates and complexes.
  • The findings indicate a conserved strategy for substrate manipulation across different chaperone families.

Conclusions:

  • PDZ-like domains represent a significant substrate-binding interface for Clp/Hsp100 molecular chaperones.
  • This interaction mechanism provides a framework for understanding how these chaperones regulate protein assembly states.
  • The study highlights a potential general principle for chaperone-mediated control over protein structures.

Related Experiment Videos