Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system [PDF]
Scientific Reports, 2018 Protein degradation is a fundamental process in all living cells and is essential to remove both damaged proteins and intact proteins that are no longer needed by the cell.
Xinying Shi +4 more
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Role of Hsp100/Clp protease complexes in controlling the regulation of motility in Bacillus subtilis [PDF]
Frontiers in Microbiology, 2016 The Hsp100/Clp protease complexes of Bacillus subtilis ClpXP and ClpCP are involved in the control of many interconnected developmental and stress response regulatory networks, including competence, redox stress response and motility.
Noel eMoliere +3 more
doaj +4 more sources
Cryo-EM structures of human ClpXP reveal mechanisms of assembly and proteolytic activation [PDF]
Nature CommunicationsThe human ClpXP complex (hClpXP) orchestrates mitochondrial protein quality control through targeted degradation of misfolded and unnecessary proteins.
Wenqian Chen +2 more
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The ClpXP protease and the ClpX unfoldase control virulence, cell division, and autolysis in Streptococcus pneumoniae [PDF]
Microbiology SpectrumIn all living cells, molecular chaperones and ATP-dependent proteases are essential for protein homeostasis. The ClpXP protease is a chaperone-protease complex conserved between bacteria and mitochondria.
Viktor H. Mebus +7 more
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NOA1, a novel ClpXP substrate, takes an unexpected nuclear detour prior to mitochondrial import. [PDF]
PLoS ONE, 2014 The mitochondrial matrix GTPase NOA1 is a nuclear encoded protein, essential for mitochondrial protein synthesis, oxidative phosphorylation and ATP production. Here, we demonstrate that newly translated NOA1 protein is imported into the nucleus, where it
Natalie Al-Furoukh +5 more
doaj +8 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
Temperature-dependent regulation of bacterial cell division hydrolases by the coordinated action of a regulatory RNA and the ClpXP protease [PDF]
The Cell SurfaceA defining feature of bacteria is the peptidoglycan cell wall which provides structural integrity and prevents osmotic lysis. While peptidoglycan hydrolases are required for daughter cell separation, dysregulated cell wall degradation may result in cell ...
Viktor H. Mebus +14 more
doaj +2 more sources
Utilizing nanoinducers for precision degradation of bacterial protein to mitigate antibiotic resistance [PDF]
Nature CommunicationsAntibiotic resistance stands as a formidable global challenge to public health. Herein, we present a bacterial nanoinducer (bacNID) designed for targeted protein degradation in treating bacterial infections. Specifically, bacNID is engineered by grafting
Linqi Han +6 more
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Targeted protein degradation in Escherichia coli using CLIPPERs [PDF]
EMBO ReportsNew, universal tools for targeted protein degradation in bacteria can help to accelerate protein function studies and antimicrobial research. We describe a new method for degrading bacterial proteins using plasmid-encoded degrader peptides which deliver ...
Matylda Anna Izert-Nowakowska +9 more
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A proteolytic AAA+ machine poised to unfold protein substrates [PDF]
Nature CommunicationsAAA+ proteolytic machines unfold proteins before degrading them. Here, we present cryoEM structures of ClpXP-substrate complexes that reveal a postulated but heretofore unseen intermediate in substrate unfolding/degradation. A ClpX hexamer draws natively
Alireza Ghanbarpour +2 more
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