Monothiol glutaredoxins: a common domain for multiple functions


DOI: 10.1007/s00018-007-6554-8

Cite this article as:
Herrero, E. & de la Torre-Ruiz, M.A. Cell. Mol. Life Sci. (2007) 64: 1518. doi:10.1007/s00018-007-6554-8


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-sulfur 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 that 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.


Glutaredoxin redox regulation glutathione oxidative stress iron-sulfur cluster transcription regulator signal transduction 

Copyright information

© Birkhäuser Verlag, Basel 2007

Authors and Affiliations

  1. 1.Departament de Ciències Mèdiques Bàsiques, IRBLLEIDAUniversitat de LleidaLleidaSpain

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