Abstract
Oxidative stress affects a wide variety of different cellular processes. Now, an increasing number of proteins have been identified that use the presence of reactive oxygen species or alterations in the cellular thiol-disulfide state as regulators of their protein function. This review focuses on two members of this growing group of redox-regulated proteins that utilize a cysteine-containing zinc center as the redox switch: Hsp33, the first molecular chaperone, whose ability to protect cells against stress-induced protein unfolding depends on the presence of reactive oxygen species and RsrA, the first anti-sigma factor that uses a cysteine-containing zinc center to sense and respond to cellular disulfide stress.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins* / chemistry
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Bacterial Proteins* / genetics
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Bacterial Proteins* / metabolism
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Cysteine / chemistry*
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Cysteine / metabolism
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Disulfides / chemistry
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Disulfides / metabolism
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Heat-Shock Proteins* / chemistry
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Heat-Shock Proteins* / metabolism
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Metalloproteins / chemistry
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Metalloproteins / metabolism
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Molecular Chaperones* / chemistry
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Molecular Chaperones* / metabolism
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Molecular Sequence Data
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Oxidation-Reduction
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Oxidative Stress
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Reactive Oxygen Species* / chemistry
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Reactive Oxygen Species* / metabolism
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Sequence Alignment
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism
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Zinc / chemistry*
Substances
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Bacterial Proteins
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Disulfides
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Heat-Shock Proteins
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Metalloproteins
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Molecular Chaperones
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Reactive Oxygen Species
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RsrA protein, Streptomyces coelicolor
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Transcription Factors
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Zinc
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Cysteine