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THIOL-BASED REGULATORY SWITCHES
Thiol-based regulatory switches play central roles in cellular responses to oxidative stress, nitrosative stress, and changes in the overall thiol-disulfide redox balance. Protein sulfhydryls offer a great deal of flexibility in the different types of modification they can undergo and the range of c...
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Published in: | Annual review of genetics 2003, Vol.37 (1), p.91-121 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Thiol-based regulatory switches play central roles in cellular responses to
oxidative stress, nitrosative stress, and changes in the overall
thiol-disulfide redox balance. Protein sulfhydryls offer a great deal of
flexibility in the different types of modification they can undergo and the
range of chemical signals they can perceive. For example, recent work on OhrR
and OxyR has clearly established that disulfide bonds are not the only cysteine
oxidation products that are likely to be relevant to redox sensing in vivo.
Furthermore, different stresses can result in distinct modifications to the
same protein; in OxyR it seems that distinct modifications can occur at the
same cysteine, and in Yap1 a partner protein ensures that the disulfide bond
induced by peroxide stress is different from the disulfide bond induced by
other stresses. These kinds of discoveries have also led to the intriguing
suggestion that different modifications to the same protein can create multiple
activation states and thus deliver discrete regulatory outcomes. In this
review, we highlight these issues, focusing on seven well-characterized
microbial proteins controlled by thiol-based switches, each of which exhibits
unique regulatory features. |
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ISSN: | 0066-4197 1545-2948 |
DOI: | 10.1146/annurev.genet.37.110801.142538 |