Results 31 to 40 of about 5,302 (190)
Intrinsic Dynamics of the ClpXP Proteolytic Machine Using Elastic Network Models
ClpXP complex is an ATP-dependent mitochondrial matrix protease that binds, unfolds, translocates, and subsequently degrades specific protein substrates. Its mechanisms of operation are still being debated, and several have been proposed, including the sequential translocation of two residues (SC/2R), six residues (SC/6R), and even long-pass ...
Lenin González-Paz +8 more
doaj +3 more sources
Cryo-EM structure of the ClpXP protein degradation machinery [PDF]
AbstractThe ClpXP machinery is a two component protease complex performing targeted protein degradation in bacteria and eukaryotes. The complex consists of the AAA+ chaperone ClpX and the peptidase ClpP. The hexameric ClpX utilizes the energy of ATP binding and hydrolysis to engage, unfold and translocate substrates into the catalytic chamber of ...
Christos Gatsogiannis +4 more
openaire +4 more sources
Post-translational regulation of the RpoS and PsrA genes in pseudomonas putida WCS358: The role of ClpXP protease [PDF]
The RpoS and PsrA proteins are key transcriptional regulators that are activated in response to the stationary phase of growth in pseudomonads. This study was designed to establish whether ClpXP (ATP-dependent serine protease) regulates levels of RpoS ...
Jovčić B. +4 more
doaj +1 more source
AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently translocated
Alireza Ghanbarpour +8 more
doaj +1 more source
Cell Sizes Matter for Industrial Bioproduction, a Case of Polyhydroxybutyrate. [PDF]
Most bacterial cells are small, restricting the accumulation of intracellular products like polyhydroxyalkanoates (PHA). To solve this problem, the ClpXP system in Halomonas bluephagenesis is identified and redesigned. Then MreB is degraded progressively by this engineered system, expanding cell size more than nine times.
Chen YL +10 more
europepmc +2 more sources
Strain-Dependent Recognition of a Unique Degradation Motif by ClpXP in
Streptococcus mutans, a dental pathogen, has a remarkable ability to cope with environmental stresses. Under stress conditions, cytoplasmic proteases play a major role in controlling the stability of regulatory proteins and preventing accumulation of ...
Biswanath Jana +2 more
doaj +1 more source
The type III secretion system (T3SS) is considered one of the major virulence factors in many bacterial pathogens. This report demonstrates that RssB, ClpXP, and RpoS play a role in T3SS regulation of Dickeya dadantii 3937. ClpP is a serine-type protease
Yan Li +8 more
doaj +1 more source
Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain [PDF]
Mitochondrial maintenance crucially depends on the quality control of proteins by various chaperones, proteases and repair enzymes. While most of the involved components have been studied in some detail, little is known on the biological role of the ...
Fischer, Fabian +3 more
core +1 more source
Discovery of antibacterial cyclic peptides that inhibit the ClpXP protease [PDF]
AbstractA method to rapidly screen libraries of cyclic peptides in vivo for molecules with biological activity has been developed and used to isolate cyclic peptide inhibitors of the ClpXP protease. Fluorescence activated cell sorting was used in conjunction with a fluorescent reporter to isolate cyclic peptides that inhibit the proteolysis of tmRNA ...
Lin, Cheng +7 more
openaire +2 more sources
The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins.
Zev A Ripstein +4 more
doaj +1 more source

