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Title:
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Monothiol glutaredoxins: a common domain for multiple functions
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Author:
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Herrero Perpiñán, Enrique; Torre Ruiz, M. A. de la
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Notes:
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Monothiol glutaredoxins with the CGFS sequence at the active site are widespread among prokaryotes and eukaryotes. Two subclasses exist, those with a single glutaredoxin domain and those with a thioredoxin-like region followed by one or
more glutaredoxin domains. Studies in Saccharomyces cerevisiae have demonstrated the role of the Grx5 protein in the biogenesis of iron-sulphur clusters. Grx5 homologues in other eukaryotes could carry out similar functions. Two S. cerevisiae monothiol glutaredoxins with the thioredoxin-like extension, Grx3 and Grx4, are modulators of the transcriptional activator Aft1, which regulates iron uptake in yeast. The human PICOT protein is a Grx3/Grx4 homologue with the same hybrid primary structure, which regulates protein kinase C activity and may participate in physiological processes such as control of cardiac function. Therefore, monothiol glutaredoxins share a common basic structural motif and biochemical mechanism of action, while participating in a diversity of cellular functions as protein redox regulators. |
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Subject(s):
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-Glutaredoxin
-Estrès oxidatiu
-Llevat de cervesa
-Estrès oxidatiu
-Saccharomyces cerevisiae |
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Rights:
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(c) Birkhäuser Verlag, 2007
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Document type:
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article
submittedVersion |
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Published by:
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Springer
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Share:
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