Reference: Izquierdo A, et al. (2008) Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway. Eukaryot Cell 7(8):1415-26

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Abstract


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 Golgi. Expression of GRX6 is modestly up-regulated by several stresses (calcium, sodium, peroxides), in a manner dependent on the Crz1-calcineurin pathway. Some of these stresses also up-regulate GRX7 expression, under the control of the Msn2/4 transcription factor. The N-glycosylation inhibitor tunicamycin induces expression of both genes and 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 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.

Reference Type
Journal Article
Authors
Izquierdo A, Casas C, Muhlenhoff U, Lillig CH, Herrero E
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