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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.
The...
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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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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

Energy to Drive Translocation

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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.
Generally, polypeptides are unfolded by two distinct...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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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...
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Updated: Oct 3, 2025

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

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ATP-Independent Chaperones.

Rishav Mitra1,2, Kevin Wu1,3, Changhan Lee4

  • 1Howard Hughes Medical Institute, University of Michigan, Ann Arbor, Michigan, USA;

Annual Review of Biophysics
|February 15, 2022
PubMed
Summary
This summary is machine-generated.

ATP-independent molecular chaperones actively influence protein folding by modulating client affinity, moving beyond their passive holdase role. This review explores their dynamic mechanisms and client interaction regulation.

Keywords:
SpySurAholdaseprotein foldingsmall heat shock proteinstrigger factor

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Protein folding is essential for biological function.
  • Molecular chaperones protect the proteome from misfolding and aggregation.
  • ATP-independent chaperones traditionally act as passive holdases.

Purpose of the Study:

  • To review emerging mechanisms of ATP-independent chaperones.
  • To discuss how these chaperones regulate client binding and release.
  • To highlight their active role in protein folding.

Main Methods:

  • Literature review of recent research on ATP-independent chaperones.
  • Analysis of studies on chaperone-client interactions.
  • Synthesis of data on chaperone functional cycles.

Main Results:

  • ATP-independent chaperones actively influence the protein folding energy landscape.
  • They tune their affinity to different client folding states.
  • Regulation of client binding and release involves diverse modes.

Conclusions:

  • ATP-independent chaperones are not merely passive holdases.
  • They play an active role in guiding protein folding.
  • Understanding their dynamic mechanisms is crucial for proteostasis research.