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Related Concept Videos

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...
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...
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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

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Related Experiment Video

Updated: May 16, 2026

Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

A tightly regulated molecular toggle controls AAA+ disaggregase.

Yuki Oguchi1, Eva Kummer, Fabian Seyffer

  • 1Zentrum für Molekulare Biologie der Universität Heidelberg, Heidelberg, Germany.

Nature Structural & Molecular Biology
|November 20, 2012
PubMed
Summary
This summary is machine-generated.

The ClpB protein

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Area of Science:

  • Protein biochemistry
  • Molecular biology
  • Chaperone-assisted protein folding

Background:

  • ClpB is an AAA+ protein crucial for refolding aggregated proteins with the DnaK system in E. coli.
  • The M domain of ClpB, a unique coiled-coil structure, is vital for disaggregation but its precise role and location within the ClpB hexamer are unclear.

Purpose of the Study:

  • To determine the structural positioning and mechanistic function of ClpB M domains within the ClpB hexamer.
  • To elucidate the regulatory mechanism governing ClpB activity through its M domains.

Main Methods:

  • Structural analysis of ClpB hexamers
  • Biochemical assays to assess ClpB activity
  • Site-directed mutagenesis to probe M domain function
  • In vivo toxicity studies

Main Results:

  • M domains are located on the ClpB ring surface, interacting with the AAA-1 ATPase domain.
  • Both M-domain motifs (1 and 2) are essential for maintaining a repressed ClpB activity state.
  • Motif 2 regulates unfolding power via intramolecular docking to AAA-1; motif 1 interacts with a neighboring AAA-1 domain.
  • Stabilizing motif 2 docking represses ClpB, while destabilization leads to toxic hyperactivation.

Conclusions:

  • ClpB activity is tightly regulated by a toggle mechanism involving M-domain interactions with AAA-1 domains.
  • The M domain acts as a critical regulator, controlling ClpB's unfolding power and preventing toxic hyperactivation.
  • Understanding this regulation is key to comprehending chaperone function in protein homeostasis.