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Updated: May 25, 2026

Efficient Sporulation of Saccharomyces cerevisiae in a 96 Multiwell Format
Published on: September 17, 2016
Interaction between Saccharomyces cerevisiae glutaredoxin 5 and SPT10 and their in vivo functions
Young-Mee Oh1, Seung-Keun Hong, Jeong-Tae Yeon
1Department of Biochemistry, Paichai University, Taejon 302-735, Republic of Korea.
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 (Grx5Δ, SPT10Δ, and Grx5ΔSPT10Δ). 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.
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