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

The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

You might also read

Related Articles

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

Sort by
Same author

A subunit vaccine for multiple respiratory viruses.

Science advances·2026
Same author

Quillaja saponaria fraction QS-18 as an adjuvant for liposomal seasonal influenza vaccines.

NPJ vaccines·2026
Same author

Glycerol-driven TNAP activation in thermogenesis and mineralization.

Nature·2026
Same author

Pharmacological inhibition of PMS2 induces MMR deficiency and response to immune checkpoint blockade.

Cancer discovery·2026
Same author

Ganglioside enhances the immunogenicity of nanoparticles displaying short synthetic tumor neoepitopes and epitopes.

Theranostics·2026
Same author

Role of the anti-Shine-Dalgarno sequence of 16S rRNA in Flavobacterium johnsoniae.

Nucleic acids research·2026
Same journal

MLAC: MicroED-assisted ligand structure analysis in complexes and its application to hERG-ligand complexes.

Journal of structural biology·2026
Same journal

Ultrastructural evidence of autophagy-related processes and mitochondrial remodeling in the myxozoan parasite Henneguya piaractus.

Journal of structural biology·2026
Same journal

Architecture and dynamics of a supramolecular oxygen transport system in human homogentisate 1,2-Dioxygenase.

Journal of structural biology·2026
Same journal

Connecting pathways between mineralized fibrocartilage and bone at the Achilles tendon insertion.

Journal of structural biology·2026
Same journal

Structural and functional characterization of thermostable EstS1 esterase for BHET degradation.

Journal of structural biology·2026
Same journal

Following the white rabbit: multiscale 2D3D correlative imaging of bone structure.

Journal of structural biology·2026
See all related articles

Related Experiment Video

Updated: May 22, 2026

A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9
08:14

A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9

Published on: August 28, 2018

ClpP: a structurally dynamic protease regulated by AAA+ proteins.

John A Alexopoulos1, Alba Guarné, Joaquin Ortega

  • 1Department of Biochemistry and Biomedical Sciences, McMaster University, 1280 Main Street West, Hamilton, Ontario, Canada L8S 4K1.

Journal of Structural Biology
|May 19, 2012
PubMed
Summary
This summary is machine-generated.

Bacterial Clp proteases degrade proteins using a ClpP protease core and ClpA/ClpX unfoldases. A new review details how these unfoldases regulate ClpP

More Related Videos

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

Related Experiment Videos

Last Updated: May 22, 2026

A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9
08:14

A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9

Published on: August 28, 2018

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

Area of Science:

  • Bacterial Physiology
  • Molecular Biology
  • Enzymology

Background:

  • Bacterial protein degradation relies heavily on Clp proteases, complexes of ClpP protease and ClpA/ClpX unfoldases.
  • ClpP forms a central chamber for proteolysis, requiring unfoldase association to process substrates.
  • Regulation of substrate entry into ClpP involves an axial gate controlled by ATPase activity.

Purpose of the Study:

  • To review current understanding of ClpA/ClpX-mediated conformational changes in ClpP.
  • To elucidate the structural mechanisms regulating the ClpP axial gate.
  • To highlight insights gained from acyldepsipeptide (ADEP) antibiotic studies.

Main Methods:

  • Review of existing structural and biochemical data on ClpP, ClpA, and ClpX.
  • Analysis of crystal structures of ClpP, including complexes with ADEPs.
  • Examination of ATPase-dependent gating mechanisms.

Main Results:

  • ClpA and ClpX induce conformational changes in ClpP to open the axial gate.
  • ADEP antibiotics mimic ClpA/ClpX interactions, activating ClpP protease activity.
  • Structural details of the ATPase-regulated gating remain incompletely understood.

Conclusions:

  • Understanding Clp protease complex assembly and regulation is crucial for bacterial physiology.
  • ADEP antibiotics offer valuable tools for probing ClpP gating mechanisms.
  • Further structural studies are needed to fully resolve ClpAP/ClpXP complex dynamics and gate regulation.