Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1-ClpP1P2 protease

The ring-forming AAA+ hexamer ClpC1 associates with the peptidase ClpP1P2 to form a central ATP-driven protease in Mycobacterium tuberculosis (Mtb). ClpC1 is essential for Mtb viability and has been identified as the target of antibacterial peptides like CyclomarinA (CymA) that exhibit strong toxici...

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Main Authors: Taylor, Gabrielle (Author) , Frommherz, Yannick (Author) , Katikaridis, Panagiotis (Author) , Layer, Dominik Christian (Author) , Sinning, Irmgard (Author) , Carroni, Marta (Author) , Weber-Ban, Eilika (Author) , Mogk, Axel (Author)
Format: Article (Journal)
Language:English
Published: August 2022
In: The journal of biological chemistry
Year: 2022, Volume: 298, Issue: 8, Pages: 1-12
ISSN:1083-351X
DOI:10.1016/j.jbc.2022.102202
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.jbc.2022.102202
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0021925822006445
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Author Notes:Gabrielle Taylor, Yannick Frommherz, Panagiotis Katikaridis, Dominik Layer, Irmgard Sinning, Marta Carroni, Eilika Weber-Ban, and Axel Mogk
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