Results 21 to 30 of about 4,851 (193)

Control of Substrate Gating and Translocation into ClpP by Channel Residues and ClpX Binding [PDF]

Journal of Molecular Biology, 2010
ClpP is a self-compartmentalized protease, which has very limited degradation activity unless it associates with ClpX to form ClpXP or with ClpA to form ClpAP. Here, we show that ClpX binding stimulates ClpP cleavage of peptides larger than a few amino acids and enhances ClpP active-site modification. Stimulation requires ATP binding but not hydrolysis
Lee, Mary E., Baker, Tania, Sauer, Robert T   +2 more
openaire   +6 more sources

A toxin/antitoxin system targeting the replication sliding-clamp induces competence in Streptococcus pneumoniae. [PDF]

PLoS Genetics
Streptococcus pneumoniae is a pathogenic bacterium capable of entering a cellular differentiation state, called competence, which enables it to acquire new genetic functions by natural transformation, as well as physiological functions such as tolerance ...
Mickaël Maziero, Dimitri Juillot, Isabelle Mortier-Barrière, Rut Carballido-Lopez, Nathalie Campo, Pierre Genevaux, Patricia Bordes, Patrice Polard, Mathieu Bergé   +8 more
doaj   +2 more sources

Disruption of the ATP-dependent unfoldase ClpX reverses antifungal resistance in Cryptococcus neoformans [PDF]

Nature Communications
Fungal diseases impact the lives of a millions of people across the globe, and with our current repertoire of therapeutic options dwindling, effective treatment strategies are urgently needed.
M. Woods, A. Bermas, B. Ball, B. Muselius, N. Chan, D. Gutierrez-Gongora, S. Ramezanpour, J. A. McAlister, S. A. Sieber, J. Geddes-McAlister   +9 more
doaj   +2 more sources

Mutations in ClpC1 or ClpX subunit of caseinolytic protease confer resistance to ilamycins in mycobacteria [PDF]

Communications Biology
The mycobacterial caseinolytic protease (Clp) system has been recognized as a promising therapeutic target. In this study, we identify two novel ilamycin analogs, ilamycin E (ILE) and ilamycin F (ILF), both targeting the ClpC1 component of the ClpC1P1P2 ...
Yamin Gao, Cuiting Fang, Biao Zhou, H. M. Adnan Hameed, Changli Sun, Xirong Tian, Jing He, Xingli Han, Han Zhang, Jun Li, Jianhua Ju, Xinwen Chen, Nanshan Zhong, Junying Ma, Xiaoli Xiong, Tianyu Zhang   +15 more
doaj   +2 more sources

Mitochondrial CLPP in Health and Disease: Mechanisms, Therapeutic Duality and Emerging Opportunities. [PDF]

J Inherit Metab Dis
The graphical abstract illustrates the context‐dependent therapeutic modulation of CLPP. Pharmacological CLPP activation has reached clinical application in cancer (black arrow), whereas reduced CLPP activity has shown beneficial effects experimentally in models of primary mitochondrial disease and metabolic syndrome, as well as cancer (grey arrows ...
Isermann L, Trifunovic A.
europepmc   +2 more sources

Elucidating the Molecular Impact of DA29‐Induced ClpP Chemoactivation on Mitochondrial Function [PDF]

FASEB J
A promising approach to tackling DIPG, a lethal pediatric brain tumor, relies on small molecules capable of activating the human mitochondrial protease hClpP. The novel piperazine‐based compound DA29 specifically activates endogenous hClpP, thereby compromising mtDNA levels, mitoribosomes, and OXPHOS complex subunits.
Rizzo F, Miciaccia M, Perrone M, Scilimati A, Polosa P, Bruni F.   +5 more
europepmc   +2 more sources

ClpX interactions with ClpP, SspB, protein substrate and nucleotide [PDF]

, 2006
ClpXP and related ATP-dependent proteases are implements of cytosolic protein destruction. They couple chemical energy, derived from ATP hydrolysis, to the selection, unfolding, and degradation of protein substrates with the appropriate degradation signals. The ClpX component of ClpXP is a hexameric enzyme that recognizes protein substrates and unfolds
Hersch, Greg Louis
openaire   +2 more sources

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, Yuan Xiao, Jingkai Gu, Peikun Zhao, Zhe Hu, Jiahuan Zheng, Renwu Hua, Zhuo Hai, Jiaping Su, Jian V. Zhang, William S. B. Yeung, Tianren Wang   +11 more
doaj   +1 more source

Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae [PDF]

FEBS Letters, 1998
Members of the Hsp100/Clp‐family of molecular chaperones form regulatory subunits of ATP‐dependent Clp proteases and fulfill crucial roles for cellular thermotolerance. We have identified a Clp‐like protein in Saccharomyces cerevisiae, Mcx1p, which shares approximately 30% sequence identity with ClpX‐proteins in bacteria, plants and nematodes.
van Dyck, L., Dembowski, M., Neupert, W., Langer, T.   +3 more
openaire   +3 more sources

Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

Cells, 2021
Biallelic pathogenic variants in CLPP, encoding mitochondrial matrix peptidase ClpP, cause a rare autosomal recessive condition, Perrault syndrome type 3 (PRLTS3). It is characterized by primary ovarian insufficiency and early sensorineural hearing loss,
Jana Key, Sylvia Torres-Odio, Nina C. Bach, Suzana Gispert, Gabriele Koepf, Marina Reichlmeir, A. Phillip West, Holger Prokisch, Peter Freisinger, William G. Newman, Stavit Shalev, Stephan A. Sieber, Ilka Wittig, Georg Auburger   +13 more
doaj   +1 more source