Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation

ClpB, a bacterial homologue of heat shock protein 104 (Hsp104), can disentangle aggregated proteins with the help of the DnaK, a bacterial Hsp70, and its co-factors. As a member of the expanded superfamily of ATPases associated with diverse cellular activities (AAA(+)), ClpB forms a hexameric ring s...

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Bibliografiset tiedot
Julkaisussa:J Biol Chem
Päätekijät: Sugita, Saori, Watanabe, Kumiko, Hashimoto, Kana, Niwa, Tatsuya, Uemura, Eri, Taguchi, Hideki, Watanabe, Yo-hei
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Society for Biochemistry and Molecular Biology 2018
Aiheet:
Protein Structure and Folding
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC6302173/
https://ncbi.nlm.nih.gov/pubmed/30327424
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.005496
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