Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates
When ribosomes fail to complete normal translation, all cells have mechanisms to ensure degradation of the resulting partial proteins to safeguard proteome integrity.
Xue Fei +4 more
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Staphylococcal toxic shock syndrome is a potentially lethal illness attributed to superantigens produced by Staphylococcus aureus, in particular toxic shock syndrome toxin 1 (TSST-1), but staphylococcal enterotoxins (SEs) are also implicated.
Jenny Schelin +3 more
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The Bacterial ClpXP-ClpB Family Is Enriched with RNA-Binding Protein Complexes
In the matrix of bacteria/mitochondria/chloroplasts, Lon acts as the degradation machine for soluble proteins. In stress periods, however, proteostasis and survival depend on the strongly conserved Clp/Hsp100 family. Currently, the targets of ATP-powered
Georg Auburger, Jana Key, Suzana Gispert
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Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker. [PDF]
ClpXP is a two-component ATP-dependent protease that unfolds and degrades proteins bearing specific recognition signals. One substrate degraded by Escherichia coli ClpXP is FtsZ, an essential cell division protein.
Jodi L Camberg +4 more
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ClpXP, an ATP-powered unfolding and protein-degradation machine
ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform mechanical work during targeted protein degradation within cells. ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP). Asymmetric ClpX hexamers bind unstructured peptide tags in protein substrates, unfold stable tertiary structure
Baker, Tania, Sauer, Robert T
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Substrate selection by the ClpXP protease : a tail of destruction [PDF]
(cont.) sites for CIpA and SspB; this spatial arrangement of signals allows for efficient modulation of proteolysis of ssrA-tagged proteins. Finally, additional substrates whose degradation may be regulated by the adaptor protein SspB were determined by identifying substrates captured in ClpXP[trap] in an sspB⁺ strain but not an sspB⁻ strain.
Flynn, Julia M., 1976-
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Survival of Anaerobic Fe 2+ Stress Requires the ClpXP Protease [PDF]
ABSTRACT Shewanella oneidensis strain MR-1 is a versatile bacterium capable of respiring extracellular, insoluble ferric oxide minerals under anaerobic conditions. The respiration of iron minerals results in the production of soluble ferrous ions, which at high concentrations are toxic to living organisms.
Brittany D, Bennett +2 more
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Mitochondrial CLPP in Health and Disease: Mechanisms, Therapeutic Duality and Emerging Opportunities. [PDF]
The graphical abstract illustrates the context‐dependent therapeutic modulation of CLPP. Pharmacological CLPP activation has reached clinical application in cancer (black arrow), whereas reduced CLPP activity has shown beneficial effects experimentally in models of primary mitochondrial disease and metabolic syndrome, as well as cancer (grey arrows ...
Isermann L, Trifunovic A.
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De Novo Discovery of Bioactive Cyclic Peptides via Cellular Selection of Genetically Encoded Libraries. [PDF]
Genetically encoded cyclic peptide libraries can be employed in cellular selection platforms to identify cyclic peptide inhibitors for therapeutic targets by directly selecting for desired biological activities. This review systematically summarizes representative studies and suggests future opportunities for using cellular selection for de novo cyclic
Yang L, Behera A, Meyers HJ, Wang T.
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CLPXP FUNCTIONS IN CAULOBACTER AS A UNIVERSAL AND SPECIES-SPECIFIC PROTEASE
This dissertation studies the representation of madness in the literary works of three twentieth-century authors, namely, João Guimarães Rosa (from Brazil), Silvina Ocampo (from Argentina), and Luis Martín-Santos (from Spain). The first chapter argues that madness in Ocampo’s “El castigo”, Rosa’s “Buriti”, and Martín-Santos, Tiempo de silencio, reveals
Vass, Robert
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