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SGT2 and MDY2 Interact with Molecular Chaperone YDJ1 in Saccharomyces Cerevisiae

Shen-Ting Liou, Ming-Yuan Cheng and Chung Wang
Cell Stress & Chaperones
Vol. 12, No. 1 (Spring, 2007), pp. 59-70
Published by: Cell Stress Society International in partnership with Springer
Stable URL: http://www.jstor.org/stable/4539749
Page Count: 12
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
SGT2 and MDY2 Interact with Molecular Chaperone YDJ1 in Saccharomyces Cerevisiae
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Abstract

In Saccharomyces cerevisiae, Sgt2 was thought to be the homologue of vertebrate SGT (small glutamine tetratricopeptide repeat-containing protein). SGT has been known to interact with both Hsp70 and Hsp90. However, it was not clear whether Sgt2 might have a similar capacity. Here, we showed that Ssal/Ssa2 (yeast heat shock cognate [Hsc]70), Hsc82 (yeast Hsp90), and Hspl104 coprecipitated with Sgt2 from yeast lysates. Another molecular chaperone, Ydjl, known to interact with Ssal and Hsc82, also coprecipitated with Sgt2. Synthetic lethality between SGT2 and YDJ1 was observed after the cells were under stress, although Sgt2 might not interact physically with Ydjl. We also found that Mdy2 interacted with the N-terminal region of Sgt2 and that Mdy2 appeared to interact physically with Ydjl. Mdy2 therefore may mediate the association of Ydjl and Sgt2. In addition, the mating efficiency of mdy2?��, sgt2?��, and mdy2?��sgt2?�� strains was reduced to a similar extent. Compared with mdy2?�� and ydjl?�� cells, ydjl?��mdy2?�� cells, however, showed a further suppression in mating efficiency. Moreover, MDY2 interacted genetically with YDJ1. These results suggest that protein complexes containing Sgt2 and Mdy2 bring molecular chaperones together to carry out certain chaperoning functions.

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