Proteomics

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Bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70-Hsp40 substrates preferentially by the HslUV protease

ABSTRACT: Whereas in eukaryotic cells Hsp90s are extensively studied in bacteria, the function of Hsp90 (HtpG) and its functional relationship with Hsp70 (DnaK) remains unknown. To uncover physiological processes depending on HtpG and DnaK, we performed comparative quantitative proteomic analyses of insoluble and total protein fractions from unstressed wild type E. coli, and from knockout mutants ΔdnaKdnaJ (ΔKJ), ΔhtpG (ΔG) and ΔdnaKdnaJΔhtpG (ΔKJG) and compared their growth rates under heat-stress also with ΔdnaKdnaJΔhslV.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Escherichia Coli

SUBMITTER: Manfredo Quadroni  

LAB HEAD: Pierre Goloubinoff

PROVIDER: PXD010014 | Pride | 2021-07-07

REPOSITORIES: Pride

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Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates.

Fauvet Bruno B   Finka Andrija A   Castanié-Cornet Marie-Pierre MP   Cirinesi Anne-Marie AM   Genevaux Pierre P   Quadroni Manfredo M   Goloubinoff Pierre P  

Frontiers in molecular biosciences 20210415

In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration with Hsp70 (DnaK) remains poorly characterized. To uncover physiological processes that depend on HtpG and DnaK, we performed comparative quantitative proteomic analyses of insoluble and total protein fractions from unstressed wild-type (WT) <i>Escheric  ...[more]

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