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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 25 for “"ClpXP"”.
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Mechanistic studies of the AAA+ molecular motor ClpXP
… 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. ClpX utilizes the energy from ATP hydrolysis to pull on bound substrates, …
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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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Substrate selection by the ClpXP protease : a tail of destruction
… determined by identifying substrates captured in ClpXP[trap] in an sspB⁺ strain but not an sspB⁻ strain. This analysis led to the identification of the N-terminal fragment of RseA, the master regulator of the extracytoplasmic stress response, as a protein whose ClpXP-mediated degradation is also …
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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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The role of ClpXP-mediated proteolysis in resculpting the proteome after DNA damage
… specific. This thesis explores the role of the ClpXP protease in the response to DNA damage. First, we determine how DNA damage affects substrate selection by ClpXP. These experiments combine quantitative proteomics and use of an inactive variant of ClpP to "trap" cellular ClpXP substrates 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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Role of communication between subunits and enzymes in ClpXP-mediated substrate unfolding and degradation
… 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 coaxially against the double-ring ClpP₁₄ peptidase. ClpXP's peptidase active sites reside in a …
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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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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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Substrate denaturation and translocation by a proteolytic machine
… peptidase partner, ClpP. Mechanistic studies of ClpXP degradation provide insight into energy-dependent proteolysis and may help elucidate how other AAA+ motors function as well. By studying the ClpXP-mediated degradation of model substrates in native and denatured forms, I investigated the role …
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Specificity and regulation of substrate degradation for a AAA+ protease
… for all forms of life. The AAA+ proteases ClpXP and ClpAP in E. coli function in this capacity by facilitating the denaturation and degradation of target substrates. These proteolytic enzymes degrade hundreds of different proteins. Determining how the activities of these proteases are …
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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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Understanding and harnessing energy-dependent proteolysis for controlled protein degradation in bacteria
… substrates as a prelude to proteolysis. The AAA+ ClpXP protease, recognizes short peptide tags (degrons) in substrate proteins either directly or with the aid of dedicated specificity factors (adaptors). The prior identification and detailed biochemical characterization of an efficient ClpXP …
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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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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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Posttranscriptional and posttranslational regulation of virulence in erwinia amylovora
… the Csr system. Second, we examined the role of ClpXP protease in virulence regulation and its potential interaction with Lon. Mutation in clpXP diminished the T3SS expression, amylovoran production and motility, resulting in delayed disease progress. Highly accumulated RpoS proteins were …
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Synthesis and Application of Boronic Acid Derivatives
… present in the mitochondria known as human ClpXP. To study the potential selective inhibition of Human ClpXP using N-terminal peptidic boronic acid, we have designed a synthetic scheme that includes?-borylation of °,?-unsaturated carbonyl compounds using Cu(I) as catalyst, °-alkylation, …
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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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Mathematical Model of the Cell Cycle Control and Asymmetry Development in Caulobacter crescentus
… CtrA. cdG is an essential component of the ClpXP pro- tease complex, which is specifically responsible for the degradation of CtrA. We propose a mathematical model for the hierarchical assembly of ClpXP complexes, together with modeling DNA replication, transcription, and protein …
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A Forward Genetic Screen Revealed the Role of POLDIP2 in Ensuring Maternal Inheritance of Mitochondrial DNA in Drosophila melanogaster
… 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 nucleoids and mtDNA. Indeed, I found that knocking …
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