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Eukaryotic Cell, August 2008, p. 1415-1426, Vol. 7, No. 8
1535-9778/08/$08.00+0     doi:10.1128/EC.00133-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Saccharomyces cerevisiae Grx6 and Grx7 Are Monothiol Glutaredoxins Associated with the Early Secretory Pathway{triangledown} ,{dagger}

Alicia Izquierdo,1 Celia Casas,1 Ulrich Mühlenhoff,2 Christopher Horst Lillig,2 and Enrique Herrero1*

Departament de Ciències Mèdiques Bàsiques, IRBLleida, Universitat de Lleida, 25008-Lleida, Spain,1 and Institut für Zytobiologie und Zytopathologie, Philipps Universität Marburg, Marburg D-35033, Germany2

Received 14 April 2008/ Accepted 15 May 2008

Saccharomyces cerevisiae Grx6 and Grx7 are two monothiol glutaredoxins whose active-site sequences (CSYS and CPYS, respectively) are reminiscent of the CPYC active-site sequence of classical dithiol glutaredoxins. Both proteins contain an N-terminal transmembrane domain which is responsible for their association to membranes of the early secretory pathway vesicles, facing the luminal side. Thus, Grx6 localizes at the endoplasmic reticulum and Golgi compartments, while Grx7 is mostly at the Golgi. Expression of GRX6 is modestly upregulated by several stresses (calcium, sodium, and peroxides) in a manner dependent on the Crz1-calcineurin pathway. Some of these stresses also upregulate GRX7 expression under the control of the Msn2/4 transcription factor. The N glycosylation inhibitor tunicamycin induces the expression of both genes along with protein accumulation. Mutants lacking both glutaredoxins display reduced sensitivity to tunicamycin, although the drug is still able to manifest its inhibitory effect on a reporter glycoprotein. Grx6 and Grx7 have measurable oxidoreductase activity in vivo, which is increased in the presence of tunicamycin. Both glutaredoxins could be responsible for the regulation of the sulfhydryl oxidative state at the oxidant conditions of the early secretory pathway vesicles. However, the differences in location and expression responses against stresses suggest that their functions are not totally overlapping.

* Corresponding author. Mailing address: Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Montserrat Roig 2, 25008 Lleida, Spain. Phone: (34) 973-702409. Fax: (34) 973-702426. E-mail: enric.herrero{at}cmb.udl.cat

{triangledown} Published ahead of print on 23 May 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, August 2008, p. 1415-1426, Vol. 7, No. 8
1535-9778/08/$08.00+0     doi:10.1128/EC.00133-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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