Results 71 to 80 of about 3,616 (191)
Chemical Inhibition of Pyocyanin Biosynthesis Attenuates Virulence of Pseudomonas aeruginosa
Anti‐virulence strategies disarm pathogens rather than killing them directly. A β‐lactone reduces pyocyanin production without affecting growth. Chemical proteomics identified PqsC as the primary target via binding to Cys129. Crystallography revealed the binding mode, and SAR yielded a chloroacetamide inhibitor with improved enzymatic potency and anti ...
Wei Ding +3 more
wiley +1 more source
Erwinia amylovora, the causal agent of fire blight disease of apple and pear, employs intracellular proteases, including Lon and ClpXP, for posttranslational regulation of various cellular proteins. It has been shown that Lon plays a critical role in E.
Youfu Zhao, Jae Hoon Lee
core +1 more source
Elucidating the Priming Mechanism of ClpXP Protease by Single-Domain Response Regulator CpdR in Caulobacter crescentus [PDF]
In Caulobacter crescentus, progression through the cell cycle is regulated by the AAA+ protease ClpXP, and there are several classes of cell-cycle substrates that require adaptors in order to be degraded.
Barker, Kimberly E
core +1 more source
Abstract Eukaryotic proteomes are regulated by the ubiquitin‐proteasome system. Unwanted proteins are tagged with ubiquitin, which is recognized by the 26S proteasome for degradation. To enter the proteasome's 20S core particle and be hydrolyzed into peptides, the substrate must be unfolded and threaded through the 19S regulatory particle.
Edwin R. Ragwan +4 more
wiley +1 more source
Communication of ClpXP protease hypersensitivity to bacteriophage mu repressor isoforms
The immunity repressor (Rep) of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. Although Rep is stable in vivo, an altered immunity repressor (Vir) encoded by virulent, trans-dominant Mu mutants is rapidly degraded by Escherichia coli ClpXP protease. Rep and Vir are degraded
D J, Welty, J M, Jones, H, Nakai
openaire +2 more sources
Visualization of Substrate Binding and Translocation by the ATP-Dependent Protease, ClpXP [PDF]
Binding and internalization of a protein substrate by E. coli ClpXP was investigated by electron microscopy. In sideviews of ATP gamma S-stabilized ClpXP complexes, a narrow axial channel was visible in ClpX, surrounded by protrusions on its distal surface. When substrate lambda O protein was added, extra density attached to this surface. Upon addition
Ortega, Joaquin +4 more
openaire +2 more sources
More than one thousand knotted protein structures have been identified so far, but the functional roles of these knots remain elusive. It has been postulated that backbone entanglement may provide additional mechanostability.
Manoj Kumar Sriramoju +3 more
doaj +1 more source
The role of ClpX in erythropoietic protoporphyria
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 +1 more source
YdcI, a LysR‐type transcription regulator in Escherichia coli, regulates loci like iraP and mqo. Its expression is induced by (p)ppGpp under stress conditions, and protein levels rise during mid‐exponential growth, connecting its role to stress response and metabolism control. ABSTRACT YdcI, a LysR‐type transcription regulator, has been associated with
Ria Basu Roy, Karin Schnetz
wiley +1 more source
A salvage pathway maintains highly functional respiratory complex I
Maintenance and quality control of the mitochondrial respiratory chain complexes responsible for bulk energy production are unclear. Here, the authors show that the mitochondrial protease ClpXP is required for the rapid turnover of the core N-module of ...
Karolina Szczepanowska +20 more
doaj +1 more source

