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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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| Gepubliceerd in: | J Biol Chem |
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| Hoofdauteurs: | , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Biochemistry and Molecular Biology
2018
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| Onderwerpen: | |
| Online toegang: | 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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