ClpP protease modulates bacterial growth, stress response, and bacterial virulence in Brucella abortus [PDF]
Veterinary Research, 2023 The process of intracellular proteolysis through ATP-dependent proteases is a biologically conserved phenomenon. The stress responses and bacterial virulence of various pathogenic bacteria are associated with the ATP-dependent Clp protease. In this study,
Dongjie Sun +11 more
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Reversible inhibition of the ClpP protease via an N-terminal conformational switch. [PDF]
Proc Natl Acad Sci U S A, 2018 Significance ClpP is a protease that degrades damaged or misfolded proteins. Consistent with its critical role in maintaining cellular homeostasis, inhibiting and dysregulating ClpP function has shown promise in fighting antibiotic resistance and in targeting cancer cells in acute myeloid leukemia.
Vahidi S +11 more
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Disrupting α-Synuclein–ClpP interaction restores mitochondrial function and attenuates neuropathology in Parkinson’s disease models [PDF]
Molecular NeurodegenerationBackground Mitochondrial dysfunction and α-Synuclein (αSyn) aggregation are defining features of Parkinson’s disease (PD), yet the mechanistic link between them remains poorly understood.
Di Hu, Xiaoyan Sun, Xin Qi
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Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules [PDF]
Journal of Biological Chemistry, 2022 Walid Houry, Mark F Mabanglo
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Bacterial warfare at the molecular level: Pseudoalteromonas sp. H2 disrupts Vibrio splendidus membrane integrity via ClpP-CheW2 regulation [PDF]
Current Research in Microbial SciencesIn mariculture ecosystems where Vibrio spp. are predominant pathogens, effective biocontrol through antagonistic probiotics remains an unresolved biological challenge. Here, the Pseudoalteromonas sp.
Ya Li +8 more
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Self-resistance mechanism to acyldepsipeptide antibiotics in the Streptomyces producer [PDF]
mBioClp proteases are ubiquitous in bacteria and play an important role in regulatory proteolysis and in maintaining protein homeostasis within the bacterial cell. They consist of a tetradecameric, proteolytic ClpP core and associated AAA+ Clp-ATPases.
Dhana Thomy +6 more
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Repurposing Birabresib to target Gram‑positive bacteria [PDF]
npj Antimicrobials and ResistanceThe threat of antibiotic-resistant bacteria is rapidly escalating, creating an urgent need for new types of antimicrobials. Although most antibiotics act by disrupting essential cellular processes, such as cell division, replication, transcription, and ...
Hazera Khatun Koly +3 more
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The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease
EMBO Molecular Medicine, 2009 A novel class of antibiotic acyldepsipeptides (designated ADEPs) exerts its unique antibacterial activity by targeting the peptidase caseinolytic protease P (ClpP). ClpP forms proteolytic complexes with heat shock proteins (Hsp100) that select and process substrate proteins for ClpP-mediated degradation. Here, we analyse the molecular mechanism of ADEP
Heike Brötz-Oesterhelt +2 more
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Systematic Engineering of Proteases in Saccharopolyspora Spinosa Reveals Synergistic Enhancement of Spinosad Biosynthesis via Substrate Flux Optimization [PDF]
Advanced ScienceNatural product biosynthesis is tightly coupled to nitrogen allocation. However, scalable strategies to amplify pathway outputs remain limited. Here, atmospheric and room temperature plasma (ARTP) mutagenesis of Saccharopolyspora spinosa yielded a high ...
Duo Jin +9 more
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Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP. [PDF]
Commun BiolAbstract Bacterial AAA+ proteases are composed of a AAA+ partner (e.g. ClpC) and an associated peptidase (e.g. ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are crucial for stress resistance and virulence.
Azinas S +6 more
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