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 +3 more sources
Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding [PDF]
eLife, 2020 Mitochondria control the activity, quality, and lifetime of their proteins with an autonomous system of chaperones, but the signals that direct substrate-chaperone interactions and outcomes are poorly understood.
Julia R Kardon +3 more
doaj +8 more sources
Diverse nature of ClpX degradation motifs in Streptococcus mutans
Microbiology SpectrumProtein homeostasis is an essential process that depends on concerted effort of different proteins involved in proper protein folding, deciding the fate of misfolded proteins by either refolding them into their proper conformation or degrading the ...
Vivek Gurung +2 more
doaj +3 more sources
The role of ClpX in erythropoietic protoporphyria
Hematology, Transfusion and Cell Therapy, 2018 Hemoglobin is an essential biological component of human physiology and its production in red blood cells relies upon proper biosynthesis of heme and globin protein.
Jared C. Whitman +2 more
doaj +5 more sources
Mycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assembly.
PLoS ONE, 2010 FtsZ assembly at the midcell division site in the form of a Z-ring is crucial for initiation of the cell division process in eubacteria. It is largely unknown how this process is regulated in the human pathogen Mycobacterium tuberculosis.
Renata Dziedzic +9 more
doaj +3 more sources
Disruption of the ATP-dependent unfoldase ClpX reverses antifungal resistance in Cryptococcus neoformans [PDF]
Nature CommunicationsFungal 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 +9 more
doaj +2 more sources
Mutations in ClpC1 or ClpX subunit of caseinolytic protease confer resistance to ilamycins in mycobacteria [PDF]
Communications BiologyThe 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 +15 more
doaj +2 more sources
mBio, 2022 Despite having a highly reduced genome, Chlamydia trachomatis undergoes a complex developmental cycle in which the bacteria differentiate between the following two functionally and morphologically distinct forms: the infectious, nonreplicative elementary
Nicholas A. Wood +4 more
doaj +3 more sources
Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX [PDF]
Journal of Molecular Biology, 2015 ATP-dependent protein remodeling and unfolding enzymes are key participants in protein metabolism in all cells. How these often-destructive enzymes specifically recognize target protein complexes is poorly understood.
Baker, Tania +4 more
core +6 more sources
A new regulator of the Staphylococcus aureus peptidoglycan hydrolase Sle1. [PDF]
PLoS GeneticsRegulation of peptidoglycan hydrolases is crucial for bacterial cell integrity, growth and division. In the bacterial pathogen Staphylococcus aureus, the amidase Sle1 is a key autolysin required for septum splitting and daughter cell separation.
Helena Veiga +3 more
doaj +2 more sources