AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control [PDF]
Nature Communications, 2015 The Clp protease complex degrades a multitude of substrates, which are engaged by a AAA+ chaperone such as ClpX and subsequently digested by the dynamic, barrel-shaped ClpP protease. Acyldepsipeptides (ADEPs) are natural product-derived antibiotics that activate ClpP for chaperone-independent protein digestion.
Gersch, Malte +11 more
openaire +5 more sources
Developing a library of HaloPROTACs targeting the ClpP protease
Proteolysis-targeting chimeras (PROTACs) have received recent attention as a new therapeutic agent that have the potential to have a great impact in drug discovery. This project focuses on developing a chemical approach to utilise caseinolytic protease proteolytic (CLpP), a mitochondrial protease, as a potential target for mitochondrial selective ...
Nani, Alexandra
core +4 more sources
Targeting mitochondrial ClpP: structural insights and therapeutic potential of ClpP agonists in cancer therapy [PDF]
Oncology ReviewsMitochondrial “powerhouses” play a central function in cellular metabolism and energy generation. Their dysregulation is directly correlated with a myriad of diseases, among them cancer. The serine protease ClpP, accompanied by its cochaperone ClpX, is a
Mowei Kong +3 more
doaj +2 more sources
The ClpP protease homologue is required for the transmission traits and cell division of the pathogen
BMC Microbiology, 2010 Background Legionella pneumophila, the intracellular bacterial pathogen that causes Legionnaires' disease, exhibit characteristic transmission traits such as elevated stress tolerance, shortened length and virulence during the transition from the ...
Zhang Qin-fen +6 more
doaj +2 more sources
Development of Antibiotics That Dysregulate the Neisserial ClpP Protease. [PDF]
ACS Infect Dis, 2020 Evolving antimicrobial resistance has motivated the search for novel targets and alternative therapies. Caseinolytic protease (ClpP) has emerged as an enticing new target since its function is conserved and essential for bacterial fitness, and because its inhibition or dysregulation leads to bacterial cell death.
Binepal G +14 more
europepmc +4 more sources
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
doaj +2 more sources
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
doaj +2 more sources
mBio, 2022 Clp proteases consist of a proteolytic, tetradecameric ClpP core and AAA+ Clp-ATPases. Streptomycetes, producers of a plethora of secondary metabolites, encode up to five different ClpP homologs, and the composition of their unusually complex Clp ...
Laura Reinhardt +7 more
doaj +1 more source
Data in Brief, 2021 Proteolytic subunit of the caseinolytic protease system of Plasmodium knowlesi (Pk-ClpP; EC 3.4.21.92) is considered a viable target for antimalarial drug development to eradicate P.
Raimalynah Abd Razak +6 more
doaj +1 more source
ClpP/ClpX deficiency impairs mitochondrial functions and mTORC1 signaling during spermatogenesis
Communications Biology, 2023 Caseinolytic protease proteolytic subunit (ClpP) and caseinolytic protease X (ClpX) are mitochondrial matrix peptidases that activate mitochondrial unfolded protein response to maintain protein homeostasis in the mitochondria.
Chenxi Guo +11 more
doaj +1 more source