Results 41 to 50 of about 5,302 (190)
SpxA1 and SpxA2 act coordinately to fine-tune stress responses and virulence in Streptococcus pyogenes [PDF]
, 2017 SpxA is a unique transcriptional regulator highly conserved among members of the phylum Firmicutes that binds RNA polymerase and can act as an antiactivator. Why some Firmicutes members have two highly similar SpxA paralogs is not understood.
Gary C. Port +4 more
core +4 more sources
Polypeptide Translocation by the AAA+ ClpXP Protease Machine
Chemistry & Biology, 2009 In the AAA+ ClpXP protease, ClpX uses repeated cycles of ATP hydrolysis to pull native proteins apart and to translocate the denatured polypeptide into ClpP for degradation. Here, we probe polypeptide features important for translocation. ClpXP degrades diverse synthetic peptide substrates despite major differences in side-chain chirality, size, and ...
Barkow, Sarah R. +3 more
openaire +4 more sources
Frontiers in Microbiology, 2021 The ClpX ATPase is critical for resistance to cell envelope targeting antibiotics in Bacillus anthracis, however, it is unclear whether this is due to its function as an independent chaperone or as part of the ClpXP protease.
Lang Zou +5 more
doaj +1 more source
Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines [PDF]
, 2017 AAA+ proteases and remodeling machines couple hydrolysis of ATP to mechanical unfolding and translocation of proteins following recognition of sequence tags called degrons.
Baker, Tania +4 more
core +1 more source
Toxins, 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 +1 more source
Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle [PDF]
, 2016 The ClpXP protease assembles in a reaction in which an ATP-bound ring hexamer of ClpX binds to one or both heptameric rings of the ClpP peptidase. Contacts between ClpX IGF-loops and clefts on a ClpP ring stabilize the complex.
Amor, Alvaro Jorge +4 more
core +1 more source
Protein purification to analyze AAA+ proteolytic machine in vitro [PDF]
, 2011 The ATP-dependent ClpXP protease of Escherichia coli consists of two subunits, the ClpP subunit, which has the proteolytic activity and the AAA+ motor ClpX, which mechanically unfolds and translocates substrates for ClpP degradation.
Rojas, Diego F.
core +2 more sources
Roles for ClpXP in regulating the circadian clock in Synechococcus elongatus [PDF]
Proceedings of the National Academy of Sciences, 2018 Significance Protein degradation is critical for modulating cellular responses to the environment. Here, we show that proteome remodeling by ClpX, ClpP1, and ClpP2 controls circadian clock function in Synechococcus elongatus PCC 7942. The results suggest that protein degradation by the ClpXP1P2 protease is
Susan E. Cohen +2 more
openaire +4 more sources
Serine phosphorylation facilitates protein degradation by the human mitochondrial ClpXP protease. [PDF]
Proc Natl Acad Sci U S AClpXP is a two-component mitochondrial matrix protease. The caseinolytic mitochondrial matrix peptidase chaperone subunit X (ClpX) recognizes and translocates protein substrates into the degradation chamber of the caseinolytic protease P (ClpP) for proteolysis. ClpXP degrades damaged respiratory chain proteins and is necessary for cancer cell survival.
Feng Y +27 more
europepmc +3 more sources
ClpXP, an ATP-powered unfolding and protein-degradation machine
Biochimica 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 +3 more sources