Results 11 to 20 of about 3,616 (191)
The Mitochondrial Unfoldase-Peptidase Complex ClpXP Controls Bioenergetics Stress and Metastasis. [PDF]
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 +7 more sources
Multistep substrate binding and engagement by the AAA+ ClpXP protease [PDF]
Proceedings of the National Academy of Sciences, 2020 Significance AAA+ proteases play key regulatory and quality control roles in all domains of life. These destructive enzymes recognize damaged, unneeded, or regulatory proteins via specific degrons and unfold them prior to processive degradation. Here, we show that Escherichia coli
Reuben A. Saunders +3 more
openaire +4 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
The Interplay of ClpXP with the Cell Division Machinery in Escherichia coli [PDF]
Journal of Bacteriology, 2011 ABSTRACT ClpXP is a two-component protease composed of ClpX, an ATP-dependent chaperone that recognizes and unfolds specific substrates, and ClpP, a serine protease. One ClpXP substrate in Escherichia coli is FtsZ, which is essential for cell division.
Jodi L, Camberg +2 more
openaire +3 more sources
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 +2 more sources
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 +5 more sources
Scientific Reports, 2021 The human mitochondrial ClpXP protease complex (HsClpXP) has recently attracted major attention as a target for novel anti-cancer therapies. Despite its important role in disease progression, the cellular role of HsClpXP is poorly characterized and only ...
Martina Meßner +13 more
doaj +2 more sources
Polypeptide Translocation by the AAA+ ClpXP Protease Machine [PDF]
Chemistry & Biology, 2009 In the AAA+ ClpXP protease, ClpX uses repeated cycles of ATP hydrolysis to pull native proteins apart and to translocate the denatured polypeptide into ClpP for degradation. Here, we probe polypeptide features important for translocation. ClpXP degrades diverse synthetic peptide substrates despite major differences in side-chain chirality, size, and ...
Barkow, Sarah R. +3 more
openaire +5 more sources
Molecular Plant-Microbe Interactions, 2010 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 +2 more sources
The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus [PDF]
Scientific Reports, 2017 Abstract In living cells intracellular proteolysis is crucial for protein homeostasis, and ClpP proteases are conserved between eubacteria and the organelles of eukaryotic cells. In Staphylococcus aureus , ClpP associates to the substrate specificity factors, ClpX and ClpC ...
Stahlhut, Steen G. +7 more
openaire +6 more sources