Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis

Publication date: 25 April 2017
Source:Cell Reports, Volume 19, Issue 4
Author(s): Flora Ambre Honoré, Vincent Méjean, Olivier Genest
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.

Graphical abstract

Teaser

Honoré et al. show that Hsp90 is essential in the model bacterium Shewanella oneidensis under heat stress, which is contrary to previously published reports. They also identify a tRNA maturation factor TilS as a client of Hsp90 that explains the essentiality of the chaperone.


from #AlexandrosSfakianakis via Alexandros G.Sfakianakis on Inoreader http://ift.tt/2q3dWhX
via IFTTT