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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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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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Updated: Jun 7, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Insights into the function and structure of the R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1)chaperone complex.

Maryama Mohamed1, Ruikai Wu2, Walid A Houry3

  • 1Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada.

Cell Stress & Chaperones
|June 5, 2026
PubMed
Summary
This summary is machine-generated.

The R2TP chaperone complex, involving RUVBL1 and RUVBL2, aids in assembling vital cellular machinery. This review details its role in diverse processes like gene regulation and cell growth.

Keywords:
ChaperonesProtein assemblyProtein foldingProtein structureR2TP

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC
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Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

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Last Updated: Jun 7, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The R2TP chaperone complex, composed of RUVBL1, RUVBL2, RPAP3, and PIH1D1, collaborates with HSP90 and HSP70.
  • It plays a crucial role in assembling macromolecular complexes essential for cell growth and proliferation.
  • Adaptors confer substrate specificity, but the exact assembly mechanism is unclear.

Purpose of the Study:

  • To review current knowledge on the R2TP complex's function.
  • To summarize its involvement in various cellular processes and complexes.
  • To examine recent structural studies of R2TP.

Main Methods:

  • Literature review of existing research on the R2TP complex.
  • Analysis of studies on R2TP's role in protein complex assembly and stabilization.
  • Examination of structural data related to R2TP and its interacting partners.

Main Results:

  • R2TP is involved in the assembly and activity of numerous complexes, including snoRNPs, snRNPs, PIKKs, and the MRN complex.
  • It contributes to ciliogenesis, circadian rhythm regulation, and transcriptional condensate formation.
  • Recent structural studies offer insights into R2TP-mediated assembly.

Conclusions:

  • The R2TP complex is a key regulator of diverse cellular functions through its role in macromolecular assembly.
  • Further structural and mechanistic studies are needed to fully elucidate R2TP's functions.
  • Understanding R2TP is critical for comprehending cell growth, proliferation, and related diseases.