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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
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Molecular Chaperones and Protein Folding03:00

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Bacterial Protein Maturation01:26

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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...
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Energy to Drive Translocation01:37

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
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Other Stress Responses in Bacteria01:30

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Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Updated: Feb 19, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Cracking the Chaperone Code: Cellular Roles for Hsp70 Phosphorylation.

Nitika1, Andrew W Truman1

  • 1Department of Biological Sciences, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.

Trends in Biochemical Sciences
|November 6, 2017
PubMed
Summary
This summary is machine-generated.

Heat shock protein 70 (Hsp70) is crucial for cell health and cancer growth. Its phosphorylation is increasingly recognized for regulating key cellular functions and responses to cancer treatments.

Keywords:
Hsp70cancerchaperoneskinasesphosphorylation

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Intracellular Refolding Assay
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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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Last Updated: Feb 19, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Intracellular Refolding Assay
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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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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Oncology

Background:

  • Heat shock protein 70 (Hsp70) functions as a molecular chaperone.
  • Hsp70 is essential for protein folding, cell viability, and cancer cell proliferation.
  • Emerging evidence indicates Hsp70 phosphorylation influences critical cellular activities.

Purpose of the Study:

  • To investigate the regulatory role of Hsp70 phosphorylation.
  • To understand how Hsp70 phosphorylation impacts cellular processes.
  • To explore the connection between Hsp70 phosphorylation and cancer therapeutics resistance.

Main Methods:

  • Phosphorylation site analysis of Hsp70.
  • Cellular assays to assess Hsp70 activity.
  • Studies on cancer cell models.

Main Results:

  • Hsp70 phosphorylation was confirmed to regulate cell cycle progression.
  • Phosphorylation of Hsp70 impacts apoptosis pathways.
  • Hsp70 phosphorylation influences protein degradation mechanisms.
  • Hsp70 phosphorylation is linked to resistance against anticancer drugs.

Conclusions:

  • Hsp70 phosphorylation is a key regulatory mechanism in cellular processes.
  • Targeting Hsp70 phosphorylation may offer new strategies for cancer therapy.
  • Further research into Hsp70 phosphorylation is warranted for understanding cancer biology.