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Updated: Aug 7, 2026

Characterizing Mammalian Zinc Transporters Using an In Vitro Zinc Transport Assay
Published on: June 2, 2023
Zinc center as redox switch--new function for an old motif
Marianne Ilbert1, Paul C F Graf, Ursula Jakob
1Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, 48109-1048, USA.
Reactive oxygen species and thiol-disulfide states regulate protein function. This review examines Hsp33 and RsrA, two redox-regulated proteins using cysteine-zinc centers as switches to control cellular stress responses.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- Oxidative stress impacts numerous cellular processes.
- Reactive oxygen species (ROS) and thiol-disulfide balance are key regulators of protein function.
- Redox-regulated proteins are increasingly recognized for their roles in cellular signaling and stress response.
Purpose of the Study:
- To review the mechanisms of two redox-regulated proteins, Hsp33 and RsrA.
- To highlight their function as molecular switches utilizing cysteine-containing zinc centers.
- To explain their roles in cellular protection against oxidative and disulfide stress.
Main Methods:
- Literature review of studies on Hsp33 and RsrA.
- Analysis of protein structure and function related to redox sensing.
- Examination of cellular pathways involving these proteins.
Main Results:
- Hsp33, a molecular chaperone, requires ROS to protect against protein unfolding.
- RsrA, an anti-sigma factor, uses a cysteine-zinc center to detect and respond to disulfide stress.
- Both proteins exemplify a novel mechanism of redox regulation via cysteine-zinc centers.
Conclusions:
- Cysteine-containing zinc centers are critical redox switches in cellular regulation.
- Hsp33 and RsrA represent key examples of proteins adapting to oxidative and disulfide stress.
- Understanding these redox-regulated proteins offers insights into cellular defense mechanisms.
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