Literature by the same author
plus at Google Scholar

Bibliografische Daten exportieren
 

The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase

Title data

Bohl, Valentin ; Hollmann, Nele Merret ; Melzer, Tobias ; Katikaridis, Panagiotis ; Meins, Lena ; Simon, Bernd ; Flemming, Dirk ; Sinning, Irmgard ; Hennig, Janosch ; Mogk, Axel:
The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase.
In: eLife. Vol. 12 (2024) . - pp. 1-26.
ISSN 2050-084X
DOI: https://doi.org/10.7554/eLife.92746

Official URL: Volltext

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 11 Apr 2024 08:49
Last Modified: 11 Apr 2024 08:53
URI: https://eref.uni-bayreuth.de/id/eprint/89294