Regulation of Antimycin Biosynthesis Is Controlled by the ClpXP Protease [PDF]
mSphere, 2020 The survival of any microbe relies on its ability to respond to environmental change. Use of extracytoplasmic function (ECF) RNA polymerase sigma (σ) factors is a major strategy enabling dynamic responses to extracellular signals.
Bohdan Bilyk +4 more
doaj +3 more sources
The Mitochondrial Unfoldase-Peptidase Complex ClpXP Controls Bioenergetics Stress and Metastasis.
PLoS Biology, 2016 Mitochondria must buffer the risk of proteotoxic stress to preserve bioenergetics, but the role of these mechanisms in disease is poorly understood.
Jae Ho Seo +12 more
doaj +5 more sources
Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates
eLife, 2020 When ribosomes fail to complete normal translation, all cells have mechanisms to ensure degradation of the resulting partial proteins to safeguard proteome integrity.
Xue Fei +4 more
doaj +3 more sources
Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex [PDF]
Nature Communications, 2021 ClpXP is the main ATP-dependent proteolytic complex in bacteria, is essential for maintaining cellular protein homeostasis and is also critical for bacterial pathogenesis.
Kamran Rizzolo +19 more
doaj +4 more sources
Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translation [PDF]
Scientific Reports, 2017 ClpXP is the major protease in the mitochondrial matrix in eukaryotes, and is well conserved among species. ClpXP is composed of a proteolytic subunit, ClpP, and a chaperone-like subunit, ClpX. Although it has been proposed that ClpXP is required for the
Yuichi Matsushima +6 more
doaj +3 more sources
Stepwise Unfolding of a β Barrel Protein by the AAA+ ClpXP Protease [PDF]
Journal of Molecular Biology, 2011 In the AAA+ ClpXP protease, ClpX uses the energy of ATP binding and hydrolysis to unfold proteins before translocating them into ClpP for degradation.
Baker, Tania +2 more
core +6 more sources
The Bacterial ClpXP-ClpB Family Is Enriched with RNA-Binding Protein Complexes
Cells, 2022 In the matrix of bacteria/mitochondria/chloroplasts, Lon acts as the degradation machine for soluble proteins. In stress periods, however, proteostasis and survival depend on the strongly conserved Clp/Hsp100 family. Currently, the targets of ATP-powered
Georg Auburger, Jana Key, Suzana Gispert
doaj +3 more sources
An open axial channel of the AAA ClpXP protease enhances degradation of specific classes of protein substrates. [PDF]
Protein SciAbstract ClpXP and other AAA proteases maintain proteostasis and regulate cellular functions by degrading misfolded, incomplete, or regulatory proteins. ClpX recognizes substrates via unstructured degron sequences, typically located at the N‐ or C‐terminus. Although five classes of degrons are known, only recognition of the ssrA tag, a C‐motif‐1 degron,
Lyu Y +4 more
europepmc +2 more sources
Degradation of MinD oscillator complexes by Escherichia coli ClpXP [PDF]
Journal of Biological Chemistry, 2021 MinD is a cell division ATPase in Escherichia coli that oscillates from pole to pole and regulates the spatial position of the cell division machinery. Together with MinC and MinE, the Min system restricts assembly of the FtsZ-ring to midcell, oscillating between the opposite ends of the cell and preventing FtsZ-ring misassembly at the poles.
Christopher J. LaBreck +6 more
openaire +3 more sources
The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia [PDF]
The Journal of Infectious Diseases, 2020 Abstract Staphylococcus aureus is a leading cause of pneumonia. We show here that the ClpXP protease involved in protein turnover is important for pathogenesis in a murine model of acute pneumonia. Staphylococcus aureus lacking this protease is attenuated in vivo, being rapidly cleared from the airway and leading to decreased immune cell
Gyu-Lee, Kim +2 more
openaire +2 more sources