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Updated: Aug 12, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
Mitochondrial molecular chaperones: their role in protein translocation
R A Stuart1, D M Cyr, E A Craig
1Institut für Physiologische Chemie der Universität München, Germany.
Abstract:
After synthesis in the cytosol, most mitochondrial proteins must traverse mitochondrial membranes to reach their functional location. During this process, proteins become unfolded and then refold to attain their native conformation after crossing the lipid bilayers. Mitochondrial molecular chaperones play an essential mechanistic role at various steps of this process. They facilitate presequence translocation, unfolding of the cytosol-localized domains of precursor proteins, movement across the mitochondrial membranes and, finally, folding of newly imported proteins within the matrix.
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