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The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase
Open accessPreprint — published as 10.7554/elife.92746.3 · Paper page
Abstract
Heat stress can cause cell death by triggering the aggregation of essential proteins. In bacteria, aggregated proteins are rescued by the canonical Hsp70/AAA+ (ClpB) bi-chaperone disaggregase. Man-made, severe stress conditions applied during e.g. food-processing represent a novel threat for bacteria by exceeding the capacity of the Hsp70/ClpB system. Here, we report on the potent autonomous AAA+ disaggregase ClpL from Listeria monocytogenes that provides enhanced heat resistance to the food-borne pathogen enabling persistence in adverse environments. ClpL shows increased thermal stability and enhanced disaggregation power compared to Hsp70/ClpB, enabling it to withstand severe heat stress and to solubilize tight aggregates. ClpL binds to protein aggregates via aromatic residues present in its N-terminal domain (NTD) that adopts a partially folded and dynamic conformation. Target specificity is achieved by simultaneous interactions of multiple NTDs with the aggregate surface. ClpL shows remarkable structural plasticity by forming diverse higher assembly states through interacting ClpL rings. NTDs become largely sequestered upon ClpL ring interactions. Stabilizing ring assemblies by engineered disulfide bonds strongly reduces disaggregation activity, suggesting that they represent storage states.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Bohl, V., Hollmann, N. M., Melzer, T., Katikaridis, P., Meins, L., Simon, B., Flemming, D., Sinning, I., Hennig, J., & Mogk, A.
- Affiliations
- University of Geneva (CH)
- Corresponding author
- Mogk, Axel
- ORCID
- Venue
- eLife
- Publisher
- openRxiv
- Published
- 2023-10-09
- Volume
- 12
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC11006417
- OpenAlex
- W4388762888
- Cited by
- 14
- References
- 1
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 3
- FWCI
- 1.24
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- eLife (publishedVersion, cc-by)
- eLife (acceptedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- European Molecular Biology Laboratory
- Deutsche Forschungsgemeinschaft (MO970/7-1)
- Heidelberg Biosciences International Graduate School
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- Listeria monocytogenes, protein aggregation, heat stress, protein disaggregation, N-terminal domain, aromatic residues, disulfide bonds, thermal stability
- MeSH terms
- Animals, Estrus, Food, Humans, Listeria monocytogenes, Neural Tube Defects, Cell Death, HSP70 Heat-Shock Proteins
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