Oh YM, et al. (2012) Interaction between Saccharomyces cerevisiae glutaredoxin 5 and SPT10 and their in vivo functions. Free Radic Biol Med 52(9):1519-30
Abstract: Glutaredoxin 5 (Grx5) is a monothiol member of the Grx family that comprises two dithiol and three monothiol members. Using a yeast two-hybrid system, we isolated a Grx5-binding protein, SPT10, which has been previously suggested to act as a global transcriptional regulator of specific histone genes. We find that among the five members of the Grx family and two members of the thioredoxin (Trx) family (Trx1 and Trx2), Grx5 alone interacts with SPT10 via an intermolecular disulfide linkage between Cys60 of Grx5 and Cys385 of SPT10. To evaluate the physiological function of the Grx5/SPT10 interaction, we investigated the phenotypes of three null mutant strains (Grx5?, SPT10?, and Grx5?SPT10?). Taken together, the results show that all of these phenotypes are probably a consequence of the disruption of the interaction between Grx5 and SPT10. From this study, we suggest an interaction between Grx5 and SPT10 via intermolecular disulfide linkage and propose a model for a role of Grx5 in the regulation of protein expression under the control of SPT10.
|Status: Published||Type: Journal Article||PubMed ID: 22326886|
Topics addressed in this paper
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|Topics||Topics not linked to Genes||Genes linked to topics|
|Large-scale protein detection|
|Protein Physical Properties|
|Protein Sequence Features|