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Showing 1 to 13 of 13 for “"AAA+ proteases"”.
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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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Structural Principles of Substrate Recognition and Unfolding by the ClpAP and ClpXP AAA+ Proteases
… in all cells. Found in all domains of life, proteases of the AAA+ (ATPases associated with diverse cellular activities) superfamily perform targeted protein degradation of specific substrates. All AAA+ proteases consist of a hexameric AAA+ unfoldase and a compartmentalized peptidase. AAA+ …
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Examination of two remarkable AAA+ proteases: unraveling substrate-enzyme interactions of the double-ringed ClpAP and direct thermal activation of HslUV proteolysis
AAA+ (ATPases associated with diverse cellular activities) proteases are degradation enzymes, which together with other molecular machines, including disaggregases and chaperones, are critical to the maintenance of cellular protein homeostasis. Different members of this quality control network …
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Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease
… proteins. Mechanoenzymes belonging to the AAA+ (ATPases associated with diverse cellular activities) superfamily are present in all domains of life and harness energy from chemical fuels to perform mechanical work by promoting conformational changes in other biological macromolecules. …
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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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Mechanistic studies of a AAA+ protease
AAA+ proteases are present in all branches of life and responsible for the energy-dependent degradation of most cytosolic proteins. Substrates for AAA+ proteases are unfolded and translocated into a compartmental peptidase. The requirement for protein unfolding raises several questions. How easily …
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The role of the N domain in substrate binding, oligomerization, and allosteric regulation of the AAA+ Lon protease
… and often harsh environments. Cells utilize proteases and chaperones to maintain their proteomes. In bacteria, most cytosolic proteolysis is performed by self-compartmentalized AAA+ proteases, which convert the chemical energy of ATP binding and hydrolysis into mechanical work to unfold and …
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Noncanonical recognition and degradation of a stable soluble protein by AAA protease FtsH
AAA+ (ATPases associated with various cellular activities) proteolytic machines help maintain and adjust the cellular proteome in response to stress or changes in nutrients. AAA+ proteases bind degradation targets and utilize ATP-powered conformational changes in the AAA+ unfoldase ring to denature …
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Cooperativity and communication in archaeal Cdc48·20S, an ancient proteolytic machine
… process essential for life and is carried out by AAA+ proteases. AAA+ unfoldases use the energy of ATP hydrolysis to power the unfolding and translocation of protein substrates into compartmentalized peptidases for regulated proteolysis. Cdc48 is a highly conserved AAA+ homohexameric unfoldase …
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Specificity and regulation of substrate degradation for a AAA+ protease
… cellular regulation 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 …
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Degradation of the E. coli small heat-shock proteins by the AAA+ protease lon : significance to protein quality-control
… chaperones, disaggregases, holdases and proteases. Many years of investigation have led to a partial understanding of how different branches of the protein quality-control network cooperate with each other to accomplish the critical task of refolding or eliminating damaged and aggregated …
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Functions of alternative ClpP subunits in Pseudomonas aeruginosa
… physiology and regulate stress responses. Clp proteases, containing a AAA+ (A̲TPases A̲ssociated with various cellular A̲ctivities) unfoldase stacked with a compartmentalized peptidase, are central to bacterial proteolysis, and use the energy of ATP hydrolysis to unfold and translocate protein …
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Control of HslUV protease function by nucleotide binding and hydrolysis
… and their target substrates. Like other AAA+ proteases, HslUV recognizes, unfolds, translocates, and degrades substrate proteins in an ATP-dependent manner. Understanding how nucleotides interact with HslU and control the activities of both HslU and HslV provides insights into the general …