Proteomics approaches to uncover the contribution of the Hsp90 chaperone in bacterial proteostasis and stress adaptation

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Protein homeostasis is controlled in every living cells by a complex network of chaperones and proteases that ensure folding or degradation of proteins. Many of them are named “heat shock proteins” (Hsp) since their role becomes more important under stress conditions. The Hsp90 is an ATP-dependent chaperone known to be involved in the virulence of some pathogenic bacteria. However, only few bacterial proteins taken in charge by Hsp90 have been identified to date. Our goal is to evaluate the importance of Hsp90 on the proteome of the bacterial model Shewanella oneidensis, and to identify new Hsp90 clients. Thus, several proteomics approaches were implemented like label free quantitative proteomics comparing wild-type and Δhsp90 strains, crosslinking (XL) strategies, and research of post-translational modifications (PTMs). We found that numerous proteins were less abundant in the Δhsp90 strain under heat stress conditions, and some of them were confirmed to be Hsp90 clients by targeted degradation tests. Additionally, a list of putative clients was provided by the XL strategy, and interestingly, some of these proteins had also been identified with the comparative proteomics strategy. The analysis of PTMs on bacterial Hsp90 and other chaperones is currently under investigation. Altogether, these experiments allowed the identification of new clients of Hsp90, and will undoubtedly lead to a better global understanding of the role of Hsp90 to control bacterial proteostasis.

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