ArticleScientific reports2017
Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Plant Heat Shock Proteins Are More Effective in Enhancing Recombinant Alcohol Dehydrogenase Activity than Bacterial OnesIranian journal of biotechnology · 2024Article
- A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.Cell biochemistry and biophysics · 2021Review
- Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain.ACS chemical biology · 2021Article
- PV1 Protein fromInternational journal of molecular sciences · 2020Article
- Protein aggregation in bacteria.FEMS microbiology reviews · 2020Review
- Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine.Nature communications · 2019Article
- Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation.The Journal of biological chemistry · 2018Article
- The amino-terminal domain ofFEBS open bio · 2018Article
- Dynamic structural states of ClpB involved in its disaggregation function.Nature communications · 2018Article
- Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
ClpB, a bacterial Hsp100, is a ring-shaped AAA+ chaperone that can reactivate aggregated proteins in cooperation with DnaK, a bacterial Hsp70, and its co-factors. ClpB subunits comprise two AAA+ modules with an interstitial rod-shaped M-domain. The M-domain regulates ClpB ATPase activity and interacts directly with the DnaK nucleotide-binding domain (NBD). Here, to clarify how these functions contribute to the disaggregation process, we constructed ClpB, DnaK, and aggregated YFP fusion proteins in various combinations. Notably, i) DnaK activates ClpB only when the DnaK substrate-binding domain (SBD) is in the closed conformation, affording high DnaK-peptide affinity; ii) although NBD alone can activate ClpB, SBD is required for disaggregation; and iii) tethering aggregated proteins to the activated ClpB obviates SBD requirements. These results indicate that DnaK activates ClpB only when the SBD tightly holds aggregated proteins adjacent to ClpB for effective disaggregation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.