Results 31 to 40 of about 3,616 (191)
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
Chance, Destiny, and the Inner Workings of ClpXP [PDF]
Cell, 2014 AAA+ proteases are responsible for protein degradation in all branches of life. Using single-molecule and ensemble assays, Cordova et al. investigate how the bacterial protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic model that recapitulates the interplay between stochastic and deterministic behaviors of
Russell, Rick, Matouschek, Andreas
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Proteolytic Queues at ClpXP Increase Antibiotic Tolerance [PDF]
ACS Synthetic Biology, 2019 Abstract Antibiotic tolerance is a widespread phenomenon that renders antibiotic treatments less effective and facilitates antibiotic resistance. Here we explore the role of proteases in antibiotic tolerance, short-term population survival of antibiotics, using queueing theory (i.e.
Heather S. Deter +5 more
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Proteolysis-Dependent Remodeling of the Tubulin Homolog FtsZ at the Division Septum in Escherichia coli. [PDF]
PLoS ONE, 2017 During bacterial cell division a dynamic protein structure called the Z-ring assembles at the septum. The major protein in the Z-ring in Escherichia coli is FtsZ, a tubulin homolog that polymerizes with GTP.
Marissa G Viola +3 more
doaj +1 more source
Elucidating the Molecular Impact of DA29‐Induced ClpP Chemoactivation on Mitochondrial Function [PDF]
FASEB JA promising approach to tackling DIPG, a lethal pediatric brain tumor, relies on small molecules capable of activating the human mitochondrial protease hClpP. The novel piperazine‐based compound DA29 specifically activates endogenous hClpP, thereby compromising mtDNA levels, mitoribosomes, and OXPHOS complex subunits.
Rizzo F +5 more
europepmc +2 more sources
Binding and Degradation of Heterodimeric Substrates by ClpAP and ClpXP [PDF]
Journal of Biological Chemistry, 2005 ClpA and ClpX function both as molecular chaperones and as the regulatory components of ClpAP and ClpXP proteases, respectively. ClpA and ClpX bind substrate proteins through specific recognition signals, catalyze ATP-dependent protein unfolding of the substrate, and when in complexes with ClpP translocate the unfolded polypeptide into the cavity of ...
Suveena, Sharma +2 more
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Nature Communications, 2023 AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently translocated
Alireza Ghanbarpour +8 more
doaj +1 more source
Roles for ClpXP in regulating the circadian clock in Synechococcus elongatus [PDF]
Proceedings of the National Academy of Sciences, 2018 Significance Protein degradation is critical for modulating cellular responses to the environment. Here, we show that proteome remodeling by ClpX, ClpP1, and ClpP2 controls circadian clock function in Synechococcus elongatus PCC 7942.
Susan E. Cohen +2 more
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Mechanistic studies of the AAA+ molecular motor ClpXP [PDF]
, 2009 ClpX is an archetypical representative of the AAA+ superfamily of enzymes that serves as the regulatory domain and motor for the ClpXP protease system. ClpX binds protein substrates via an amino acid sequence known as a tag, denatures them, and translocates them into the associated peptidase, ClpP.
Barkow, Sarah Rebecca
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Post-translational regulation of the RpoS and PsrA genes in pseudomonas putida WCS358: The role of ClpXP protease [PDF]
Archives of Biological Sciences, 2008 The RpoS and PsrA proteins are key transcriptional regulators that are activated in response to the stationary phase of growth in pseudomonads. This study was designed to establish whether ClpXP (ATP-dependent serine protease) regulates levels of RpoS ...
Jovčić B. +4 more
doaj +1 more source