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Molecular Chaperones and Protein Folding03:00

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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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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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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Updated: Sep 4, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Trigger factor both holds and folds its client proteins.

Kevin Wu1, Thomas C Minshull2, Sheena E Radford2

  • 1Department of Molecular, Cellular, and Developmental Biology and Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI, USA.

Nature Communications
|July 15, 2022
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Summary
This summary is machine-generated.

Trigger factor, an ATP-independent chaperone, actively prevents protein aggregation and facilitates folding. It binds partially folded GAPDH, promoting its native tetramer formation and enzymatic activity.

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Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Chaperone Function

Background:

  • ATP-independent chaperones, such as trigger factor, are traditionally viewed as passive holding chaperones.
  • Their primary role is to bind unfolded or partially folded proteins, preventing aggregation.

Purpose of the Study:

  • To investigate the active role of trigger factor in protein folding beyond its assumed passive function.
  • To elucidate the mechanism by which trigger factor influences the folding pathway of glyceraldehyde 3-phosphate dehydrogenase (GAPDH).

Main Methods:

  • Binding assays to observe trigger factor interaction with partially folded GAPDH.
  • Monitoring protein folding intermediates and oligomerization states.
  • Assessing enzymatic activity of folded GAPDH.

Main Results:

  • Trigger factor binds to partially folded GAPDH, shielding oligomeric interfaces and inhibiting aggregation.
  • GAPDH folds into a native-like monomeric intermediate while bound to trigger factor.
  • Released GAPDH rapidly forms its native tetramer and regains enzymatic activity without additional folding factors.

Conclusions:

  • Trigger factor actively participates in protein folding, not just holding.
  • The study proposes a novel mechanism where trigger factor bridges holding and folding chaperone activities.
  • This active role contributes to efficient protein maturation and function.