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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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Trigger factor chaperone acts as a mechanical foldase.

Shubhasis Haldar1, Rafael Tapia-Rojo2, Edward C Eckels3

  • 1Department of Biological Sciences, Columbia University, New York, NY, 10027, USA. sh3529@columbia.edu.

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|September 24, 2017
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Summary
This summary is machine-generated.

Molecular chaperones like trigger factor help proteins fold correctly under mechanical stress. This study shows trigger factor acts as a mechanical foldase, crucial for processes like co-translational folding.

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Area of Science:

  • Molecular biology
  • Biophysics

Background:

  • Proteins undergo mechanical forces during essential biological processes such as muscle contraction and co-translational folding.
  • Mechanical force can impede protein folding, necessitating the involvement of molecular chaperones.
  • The precise role of chaperones in protein folding under force has remained largely uninvestigated.

Purpose of the Study:

  • To investigate the influence of the molecular chaperone trigger factor on the folding dynamics of protein L under physiological forces.
  • To determine if trigger factor can facilitate protein folding against mechanical force.

Main Methods:

  • Utilized single-molecule magnetic tweezers to apply controlled forces (4-10 pN) to protein L.
  • Monitored the folding and refolding kinetics of protein L in the presence and absence of trigger factor.

Main Results:

  • Trigger factor significantly enhanced the probability of protein L folding under applied mechanical force.
  • Trigger factor accelerated the refolding kinetics of protein L.
  • The chaperone's ability to aid folding was force-dependent, requiring higher concentrations at greater forces.

Conclusions:

  • Molecular chaperones, exemplified by trigger factor, can function as 'mechanical foldases,' actively promoting protein folding under force.
  • This chaperone-assisted folding mechanism under force is potentially significant for various physiological processes, including co-translational folding at the ribosome.