Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates
| Autor: | Andrija Finka, Manfredo Quadroni, Pierre Goloubinoff, Bruno Fauvet, Pierre Genevaux, Anne-Marie Cirinesi, Marie-Pierre Castanié-Cornet |
|---|---|
| Přispěvatelé: | Université de Lausanne (UNIL), University of Zadar, Laboratoire de microbiologie et génétique moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre de recherche en pharmacologie - santé (CRPS), Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
MESH: Mycobacterium tuberculosis
SecB medicine.medical_treatment Mutant ClpX MESH: Escherichia coli Proteins MESH: Protein Isoforms medicine.disease_cause Biochemistry DnaJ DnaK MESH: Recombinant Proteins 0302 clinical medicine MESH: Genetic Vectors MESH: Endopeptidase Clp Molecular Biosciences Toxin-antitoxin Biology (General) MESH: Bacterial Proteins Original Research 0303 health sciences MESH: Gene Expression Regulation Bacterial biology Chemistry MESH: Escherichia coli HslV Hsp90 MESH: ATPases Associated with Diverse Cellular Activities MESH: Bacterial Genome MESH: Molecular Chaperones Proteases MESH: Gene Expression HtpG chaperones proteostasis QH301-705.5 MESH: Proteolysis Biochemistry Genetics and Molecular Biology (miscellaneous) 03 medical and health sciences HigB1-HigA1 chaperones DnaK DnaJ proteostasis HslV HtpG Heat shock protein [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] medicine MESH: Cloning Molecular Molecular Biology Escherichia coli 030304 developmental biology Protease [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Hsp70 Proteostasis biology.protein ClpC1 030217 neurology & neurosurgery MESH: Toxin-Antitoxin Systems |
| Zdroj: | Frontiers in Molecular Biosciences Frontiers in Molecular Biosciences, Frontiers Media, 2021, 8 (14), pp.2914-2928.e7. ⟨10.3389/fmolb.2021.653073⟩ Frontiers in Molecular Biosciences, Vol 8 (2021) Frontiers in molecular biosciences, vol. 8, pp. 653073 |
| ISSN: | 2296-889X |
| DOI: | 10.3389/fmolb.2021.653073⟩ |
| Popis: | 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) Escherichia coli and from knockout mutants ΔdnaKdnaJ (ΔKJ), ΔhtpG (ΔG), and ΔdnaKdnaJΔhtpG (ΔKJG). Whereas the ΔG mutant showed no detectable proteomic differences with wild-type, ΔKJ expressed more chaperones, proteases and ribosomes and expressed dramatically less metabolic and respiratory enzymes. Unexpectedly, we found that the triple mutant ΔKJG showed higher levels of metabolic and respiratory enzymes than ΔKJ, suggesting that bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70–Hsp40 substrates. Further in vivo experiments suggest that such Hsp90-mediated degradation possibly occurs through the HslUV protease. |
| Databáze: | OpenAIRE |
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