Results 21 to 30 of about 3,616 (191)

Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates

open access: yeseLife, 2020
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
doaj   +4 more sources

A Functional ClpXP Protease is Required for Induction of the Accessory Toxin Genes, tst, sed, and sec

open access: yesToxins, 2020
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
doaj   +2 more sources

The Bacterial ClpXP-ClpB Family Is Enriched with RNA-Binding Protein Complexes

open access: yesCells, 2022
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
doaj   +3 more sources

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]

open access: yesPLoS ONE, 2014
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
doaj   +2 more sources

ClpXP, an ATP-powered unfolding and protein-degradation machine

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2012
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
openaire   +5 more sources

Substrate selection by the ClpXP protease : a tail of destruction [PDF]

open access: yes, 2004
(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-
openaire   +2 more sources

Survival of Anaerobic Fe 2+ Stress Requires the ClpXP Protease [PDF]

open access: yesJournal of Bacteriology, 2018
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
openaire   +3 more sources

Mitochondrial CLPP in Health and Disease: Mechanisms, Therapeutic Duality and Emerging Opportunities. [PDF]

open access: yesJ Inherit Metab Dis
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.
europepmc   +2 more sources

De Novo Discovery of Bioactive Cyclic Peptides via Cellular Selection of Genetically Encoded Libraries. [PDF]

open access: yesChembiochem
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.
europepmc   +2 more sources

CLPXP FUNCTIONS IN CAULOBACTER AS A UNIVERSAL AND SPECIES-SPECIFIC PROTEASE

open access: yes, 2018
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
openaire   +2 more sources

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