Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 27 for “"ClpX"”.
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ClpX interactions with ClpP, SspB, protein substrate and nucleotide
ClpXP and related ATP-dependent proteases are implements of cytosolic protein destruction. They couple chemical energy, derived from ATP hydrolysis, to the selection, unfolding, and degradation of protein substrates with the appropriate degradation signals. The ClpX component of ClpXP is a …
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Mechanism and consequences of Mu transpososome remodeling by the ClpX chaperone
E. coli ClpX is a member of the Clp/Hsp100 family of ATPases that remodel multi-component complexes and facilitate ATP-dependent protein degradation. Protein remodelers alter the biological activity of their substrates, typically by changing the quaternary structure of their target proteins. ClpX …
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Regulation of ClpP : role of substrate gating and activation by ClpX
… symmetry and sequestered active sites. ClpXP is a model self-compartmentalized protease composed of the regulator ClpX and the serine protease ClpP. Proteolysis occurs by ClpX-dependent substrate selection, unfolding, and translocation into the degradation lumen of ClpP, where rapid and …
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Auto-tethering as a selection mechanism for recognition of multimeric substrates by the AAA+ unfoldase ClpX
The CIp/Hsp1OO enzymes, which belong to the AAA+ family of ATPases, use their unfoldase activity to degrade and remodel multimeric substrates in the bacterial cell. The mechanical energy exerted by CIp/Hsp1OO enzymes drives forward essential transitions in important biological processes. However, …
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Design framework of the MuA remodeling signal that confers preferential complex disassembly by the AAA+ unfoldase ClpX
… and disassembly reactions. Using E.coli ClpX as a model for AAA+ ATPases, I characterized the mechanism by which ClpX discriminates between two oligomeric states of one of its natural multimeric substrates, phage MuA tranposase. I elucidated many strategies for ClpX's preference for the …
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Quantifying the Release of Protein Substrates from AAA+ ATPase ClpX by Single Molecule Total Internal Reflection Fluorescence Microscopy
… release of the substrate using the AAA+ ATPase ClpXP. We present a new assay based on Total-Internal-Reflection Fluorescence (TIRF) microscopy that measures the lifetime of the ClpX-substrate complex. We demonstrate that the technique has the potential to identify factors that affect the mean …
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Role of communication between subunits and enzymes in ClpXP-mediated substrate unfolding and degradation
… of energy-dependent proteases. For example, the ClpX ATPase disassembles macromolecular complexes and combines with the ClpP peptidase to form ClpXP, a molecular machine with structural and functional similarity to the eukaryotic 26S proteasome. ClpXP consists of hexameric ClpX rings stacked …
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Mechanistic studies of the AAA+ molecular motor ClpXP
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. …
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Dissecting the steps of substrate processing by the energy-dependent protease ClpXP
… In the bacterial energy-dependent protease ClpXP, ClpX is the regulatory component and ClpP is the proteolytic component. To better understand the proteolytic activity of ClpXP we investigated the steps involved in processing of substrates by ClpXP. The aim of this thesis is to present …
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Single-molecule studies of protein degradation and kinesin-8 motility
… machine functions, using two biological systems: ClpXP proteases and kinesin-8 Kif18B. As members of bigger protein families, these two fascinating nanomachines perform important cellular tasks in protein quality control and spindle formation, respectively. AAA+ ClpX unfoldases use energy from ATP …
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Mechanistic studies of a AAA+ protease
… into mechanical unfolding and translocation? ClpXP is a AAA+ protease that consists of the hexameric ClpX unfoldase and polypeptide translocase and the ClpP compartmental peptidase. ClpX binds a substrate by an unstructured degradation tag and then, by multiple rounds of ATP-binding and …
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Identifying the requirement and mechanism of the dynamic yet kinetically stable ClpXP interface
… limited. The subject of this thesis is the AAA+ ClpXP protease from Escherichia coli. ClpX is a AAA+ hexamer, and ClpP is a self-compartmentalized peptidase. Previous experiments have shown that ATP is required for assembly of active ClpXP complexes. Moreover, the IGF loops of ClpX are known to …
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Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine
… and regulation in all domains of life. ClpX, a AAA+ ring homohexamer, uses the energy of ATP binding and hydrolysis to power conformational changes that unfold and translocate target proteins into the ClpP peptidase for degradation. X-ray crystal structures show that some ClpX subunits …
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Characterization of the interaction between FtsZ-ring stabilizer ZapC and the conserved protease ClpXP in E. coli cytokinesis
… ZapC may be a substrate of the cellular protease ClpXP in E. coli. The conserved molecular chaperone ClpXP is responsible for degradation of a wide range of substrates, including FtsZ in E. coli. Here, we show that that ZapC and ClpX proteins interact in a bacterial two-hybrid (BACTH) assay. A …
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Untersuchungen zum Einfluss der ATP-abhängigen Protease ClpXP auf die Regulation und Expression Virulenz-assoziierter Gene des uropathogenen E. coli Stammes 536
Die ATP-abhängige Serinprotease ClpXP ist für die Kontrolle und Verfügbarkeit einer großen Anzahl von Enzymen und regulatorischer Proteine sowie für den Abbau fehlge-falteter Proteine verantwortlich. Sie besteht aus zwei Komponenten, der Protease ClpP und der ATPase ClpX, welche für die …
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Single molecule fluorescence spectroscopy of ClpXP-mediated substrate degradation
Energy-dependent proteases, such as ClpXP, are responsible for the regulated destruction of proteins in prokaryotes and organelles of eukaryotes. AAA+ ATPases in these proteases recognize protein substrates and power their mechanical denaturation and subsequent translocation into a sequestered …
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A Forward Genetic Screen Revealed the Role of POLDIP2 in Ensuring Maternal Inheritance of Mitochondrial DNA in Drosophila melanogaster
… to the mitochondrial matrix and interacts with ClpX, a chaperone-like subunit of the major protease ClpXP in the mitochondria. Mutation of POLDIP2 was previously shown to result in alteration of the cellular levels and activity of ClpXP in human cells, which could affect the maintenance of …
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Structural Principles of Substrate Recognition and Unfolding by the ClpAP and ClpXP AAA+ Proteases
… by the bacterial AAA+ proteases ClpAP and ClpXP, which are composed of either the double-ringed ClpA or the single-ring ClpX unfoldase in complex with the ClpP peptidase. Using covalently crosslinked ClpA–ClpP complexes, I interrogate the symmetry mismatch between the ClpA hexamer and the …
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Functions of alternative ClpP subunits in Pseudomonas aeruginosa
… differentially with the AAA+ unfoldases, ClpX and ClpA. Finally, the PaClpP2 peptide-cleavage active site uniquely contributes to P. aeruginosa biofilm development. Therefore, results presented in this thesis suggest that within AAA+ proteases, the specificity of the peptidase subunits, …
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Binding with intent to destroy : RssB adaptor function in Clp-XP-mediated proteolysis of sigmaS
… focus on the facilitated delivery of as to the ClpXP protease. Proteolysis of as by ClpXP requires the accessory factor RssB. RssB is a two-component response regulator. Not surprisingly, its activity is positively regulated by phosphorylation of a conserved aspartate in its receiver domain. …
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