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Showing 1 to 20 of 22 for “"AAA ATPase"”.
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Quantifying the Release of Protein Substrates from AAA+ ATPase ClpX by Single Molecule Total Internal Reflection Fluorescence Microscopy
… process for maintaining proteostasis in cells. AAA+ proteases, such as proteasomes, play a major role in selective degradation of proteins. Degradation by AAA+ proteases typically requires the substrate to be physically unfolded before proteolysis. The efficiency of the unfolding process is …
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Sequential Actions of VCP/p97 and the Proteasome 19S Regulatory Particle in Sterol-Accelerated, ER-Associated Degradation of HMG CoA Reductase
… through poorly defined reactions mediated by the AAA-ATPase VCP/p97 and augmented by the nonsterol isoprenoid geranylgeraniol. Here, we report that the oxysterol 25-hydroxycholesterol and geranylgeraniol combine to trigger extraction of reductase across ER membranes prior to its cytosolic release. …
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Design framework of the MuA remodeling signal that confers preferential complex disassembly by the AAA+ unfoldase ClpX
… non-native states. The Clp/Hsp100 family of ATPases are unfolding chaperones that remodel macromolecular complexes and facilitate ATP-dependent protein degradation. They are members of the superfamily of AAA+ enzymes (ATPases Associated with various cellular Activities), which is conserved …
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Substrate denaturation and translocation by a proteolytic machine
Many AAA+ molecular machines generate power and drive cellular processes by harnessing energy from cycles of ATP hydrolysis. ClpX is a relatively simple AAA+ ATPase that powers regulated protein degradation by binding native protein substrates, denaturing them, and translocating the unfolded …
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The molecular basis of LINC complex formation
… also arise from the structure. TorsinA is an AAA+ ATPase suggested to play a role in LINC complex regulation. Analysis of Torsin's binding partners LAP1 and LULL1 show that they are catalytically inactive AAA+ ATPases. We characterize the complex and show by EM that they form ring akin to …
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Functional and structural studies of AAA+ proteases
AAA+ proteases are found in all domains of life. They degrade misfolded proteins as well as specific regulatory factors and thus play critical roles in protein quality control and numerous cellular processes. These enzymes share a conserved architecture in which a hexameric AAA+ ATPase recognizes, …
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The establishment and characterization of an improved cell-free assay for exocytosis in neuroendocrine PC12 cells
… in einer konzertierten Aktion von α-SNAP und der AAA-ATPase NSF dissoziiert wird. In dieser Arbeit wurde ein zellfreier Exozytose-Assay entwickelt.Auf beschichteten Objektträgern wachsende PC12-Zellen wurden durch einen Ultraschallpuls in einer kleinen Kammer direkt auf dem Objekttisch eines …
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The Roles of the Mcm2-7 Tails in Replication Initiation
… six related subunits. Each subunit contains an AAA+ ATPase domain, a large OB-fold domain, and extensions of varying lengths on each terminus. Importantly, Mcm2, Mcm4, and Mcm6 contain long unstructured N-terminal tails, which are unrelated to each other and whose role in replication initiation …
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Protein quality control in the mammalian endoplasmic reticulum
… the misfolded protein. UBXD8 recruits p97, the AAA+ ATPase responsible for membrane extraction of dislocated proteins, to the ER using its UBX domain. UBC6e is a membrane-anchored E2 ubiquitin conjugating enzyme. AUP1 recruits a second E2, soluble UBE2G2. Additionally, AUPI regulates substrate …
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A STRUCTURAL AND FUNCTIONAL ATLAS OF THE HUMAN RIXOSOME COMPLEX
… (RNA kinase), SENP3 (SUMO protease), and MDN1 (AAA+-ATPase motor). The rixosome also has conserved RNA processing functions at heterochromatin, effectively triggering polycomb gene silencing. It has become increasingly clear that the seven protein members of the rixosome stably associate with …
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The proteasome and its ancillary proteins
… studied the proteasome interaction with the P97 AAA+ ATPase. Using the baculovirus mediated insect cell overexpression system, I recombinantly co-expressed the human P97 and the 20S proteolytic core of the proteasome. Although P97 was shown to co-purify with affinity tagged 20S proteasomes, the …
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Analyzing Resistance to Design Chemical Inhibitors of AAA Proteins
… design of chemical probes for proteins from the AAA (ATPase Associated with diverse cellular Activities) superfamily, for which only a few inhibitors are available. As the number of inhibitor-bound models of AAA proteins is also limited, the key protein-inhibitor interactions needed for design of …
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Interaction between the AAA+ protease CIpXP and the adaptor protein SspB
… protease complexes, each consisting of a AAA+ ATPase and a peptidase component. Substrate selection by the proteases is a highly regulated process to ensure minimal errant protein degradation. Substrates are usually recognized by proteases through degradation tags or degrons. Accessory …
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Chemical Biology of Dynein
<p>Cytoplasmic dynein is a AAA (ATPase Associated with various Activities) motor protein that transports cellular cargoes towards the microtubule minus-end. Despite its essential role in intracellular transport, dynein remains the least understood cytoskeletal motor. With speeds >25 μm/min in …
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The mechanism of cyclic proteasome-mediated protein degradation in Sulfolobus acidocaldarius
… B1 and B2, II) the proteasome, III) the PAN AAA+ ATP-ase, IV) Ubiquitin-like proteins in this process. In doing so, I show that C terminal region of CdvB is responsible for CdvB’s susceptibility to degradation at division. Further, my data suggest that the signal triggering CdvB is complex …
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Molecular analysis of vesicle biogenesis during autophagy
… supports the function of the previously excluded AAA+ ATPase Cdc48 in autophagic membrane fusion events.
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Biophysical Characterization of SNARE Complex Disassembly Catalyzed by NSF and alphaSNAP
… der SNARE-Komplexe durch ein Enzym, die AAA ATPase NSF sowie ihren Kofaktor SNAP vermittelt. Dazu binden vermutlich drei SNAP-Molekuele einen SNARE-Komplex und bilden so ein Podest, das als Angriffsstelle fuer das hexamere, ringfoermige NSF dient.Das Ziel der vorliegenden Arbeit war es, …
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Chemical Biology, Biochemical and Structural Studies of MDN1, an AAA Protein Required for Ribosome Biogenesis
… factors. Energy-harnessing enzymes, such as ATPases and GTPases, are needed to remodel the precursors of ribosomes at fast time scales. Mdn1 is an essential dynein-like AAA protein (ATPases Associated with various Activities) that releases specific assembly factors from the precursors of 60S …
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