Results 31 to 40 of about 5,899 (155)
Cell Division Protein FtsZ Is Unfolded for N-Terminal Degradation by Antibiotic-Activated ClpP
Antibiotic acyldepsipeptides (ADEPs) deregulate ClpP, the proteolytic core of the bacterial Clp protease, thereby inhibiting its native functions and concomitantly activating it for uncontrolled proteolysis of nonnative substrates.
Nadine Silber +5 more
doaj +1 more source
The ClpX ATPase is critical for resistance to cell envelope targeting antibiotics in Bacillus anthracis, however, it is unclear whether this is due to its function as an independent chaperone or as part of the ClpXP protease.
Lang Zou +5 more
doaj +1 more source
ClpA mediates directional translocation of substrate proteins into the ClpP protease [PDF]
The intracellular degradation of many proteins is mediated in an ATP-dependent manner by large assemblies comprising a chaperone ring complex associated coaxially with a proteolytic cylinder, e.g., ClpAP, ClpXP, and HslUV in prokaryotes, and the 26S proteasome in eukaryotes. Recent studies of the chaperone ClpA indicate that it
B G, Reid +3 more
openaire +2 more sources
Mitofusin-2 Down-Regulation Predicts Progression of Non-Muscle Invasive Bladder Cancer
Identification of markers predicting disease outcome is a major clinical issue for non-muscle invasive bladder cancer (NMIBC). The present study aimed to determine the role of the mitochondrial proteins Mitofusin-2 (Mfn2) and caseinolytic protease P ...
Antonella Cormio +9 more
doaj +1 more source
Metabolic Perturbations in a Bacillus subtilis clpP Mutant during Glucose Starvation
Proteolysis is essential for all living organisms to maintain the protein homeostasis and to adapt to changing environmental conditions. ClpP is the main protease in Bacillus subtilis, and forms complexes with different Clp ATPases.
Daniel Schultz +3 more
doaj +1 more source
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
Identification of an Unusual Intein in Chloroplast ClpP Protease of Chlamydomonas eugametos [PDF]
The proteasome-like ClpP protease is widely distributed and structurally conserved among bacteria and eukaryotic cell organelles. In Chlamydomonas eugametos, however, the chloroplast clpP gene predicted a much larger ClpP protein containing large insertion sequences (ISs).
S, Wang, X Q, Liu
openaire +2 more sources
Regulation of Cyclic Lipopeptide Biosynthesis inPseudomonas fluorescensby the ClpP Protease [PDF]
ABSTRACTCyclic lipopeptides produced byPseudomonasspecies exhibit potent surfactant and broad-spectrum antibiotic properties. Their biosynthesis is governed by large multimodular nonribosomal peptide synthetases, but little is known about the genetic regulatory network.
de Bruijn, I., Raaijmakers, J.M.
openaire +2 more sources
Structural insights into the Clp protein degradation machinery
The Clp protease system is important for maintaining proteostasis in bacteria. It consists of ClpP serine proteases and an AAA+ Clp-ATPase such as ClpC1.
Xiaolong Xu +5 more
doaj +1 more source
ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP
AAA+ proteases perform regulated protein degradation in all kingdoms of life and consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase.
Sora Kim +4 more
doaj +1 more source

