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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...

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Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
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Assembly chaperones: a perspective.

R John Ellis1

  • 1School of Life Sciences, University of Warwick, Coventry CV4 7AL, UK. r.j.ellis@warwick.ac.uk

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|March 27, 2013
PubMed
Summary
This summary is machine-generated.

Molecular chaperones assist protein folding and assembly. This review clarifies folding vs. assembly chaperones, detailing histone chaperones and their role in enzyme production.

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Area of Science:

  • Molecular biology
  • Biochemistry
  • Cell biology

Background:

  • The molecular chaperone concept has evolved significantly.
  • Distinguishing between folding and assembly chaperones is crucial for understanding protein homeostasis.
  • Misconceptions about chaperone function persist in scientific literature.

Purpose of the Study:

  • To present the historical origins and current interpretation of the molecular chaperone concept.
  • To emphasize the distinction between folding chaperones and assembly chaperones.
  • To clarify basic terminology and address misconceptions in the field.

Main Methods:

  • Literature review and conceptual analysis.
  • Discussion of historical context and current scientific understanding.
  • Detailed examination of specific chaperone examples.

Main Results:

  • The molecular chaperone concept encompasses distinct roles in protein folding and assembly.
  • Histone chaperones play critical roles in fundamental nuclear processes.
  • Assembly chaperones collaborate with folding chaperones in essential enzymatic pathways.

Conclusions:

  • A clear distinction between folding and assembly chaperones is essential for accurate scientific understanding.
  • Assembly chaperones are vital for complex biological processes, including DNA replication and gene expression.
  • Further research into chaperone mechanisms will advance our understanding of cellular function and disease.