AI Article Synopsis
- Mitochondrial proteins are essential for proper mitochondrial function, and cysteine residues play a key role in their import, folding, and activity regulation through reversible oxidation reactions.
- Cysteine oxidation is critical during the import of intermembrane space proteins, facilitating their folding and movement across the outer membrane.
- This text outlines methods to study cysteine redox states in live cells, allowing for the observation of protein import driven by oxidation and the impact of oxidative stress on mature proteins and thiol-dependent enzymes.
Article Abstract
Import, folding, and activity regulation of mitochondrial proteins are important for mitochondrial function. Cysteine residues play crucial roles in these processes as their thiol groups can undergo (reversible) oxidation reactions. For example, during import of many intermembrane space (IMS) proteins, cysteine oxidation drives protein folding and translocation over the outer membrane. Mature mitochondrial proteins can undergo changes in the redox state of specific cysteine residues, for example, as part of their enzymatic reaction cycle or as adaptations to changes of the local redox environment which might influence their activity. Here we describe methods to study changes in cysteine residue redox states in intact cells. These approaches allow to monitor oxidation-driven protein import as well as changes of cysteine redox states in mature proteins during oxidative stress or during the reaction cycle of thiol-dependent enzymes like oxidoreductases.
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| http://dx.doi.org/10.1007/978-1-4939-6824-4_8 | DOI Listing |
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