Abstract：
:The Hsp90 chaperone is essential in eukaryotes and activates a large array of client proteins. In contrast, its role is still elusive in bacteria, and only a few Hsp90 bacterial clients are known. Here, we found that Hsp90 is essential in the model bacterium Shewanella oneidensis under heat stress. A genetic screen for Hsp90 client proteins identified TilS, an essential protein involved in tRNA maturation. Overexpression of TilS rescued the growth defect of the hsp90 deletion strain under heat stress. In vivo, the activity and the amount of TilS were significantly reduced in the absence of Hsp90 at high temperature. Furthermore, we showed that Hsp90 interacts with TilS, and Hsp90 prevents TilS aggregation in vitro at high temperature. Together, our results indicate that TilS is a client of Hsp90 in S. oneidensis. Therefore, our study links the essentiality of bacterial Hsp90 at high temperature with the identification of a client.
journal_name
Cell Repjournal_title
Cell reportsauthors
Honoré FA,Méjean V,Genest Odoi
10.1016/j.celrep.2017.03.082subject
Has Abstractpub_date
2017-04-25 00:00:00pages
680-687issue
4issn
2211-1247pii
S2211-1247(17)30459-Xjournal_volume
19pub_type
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