Results 171 to 180 of about 5,327 (202)

IraM remodels the RssB segmented helical linker to stabilize σ^s against degradation by ClpXP. [PDF]

J Biol Chem
Brugger C, Srirangam S, Deaconescu AM.
europepmc   +1 more source

<i>In vitro</i> reconstitution of biological oscillators. [PDF]

Front Cell Dev Biol
van der Vlist E, de Vries S, Kamenz J.
europepmc   +1 more source

Regulatory Components for Bacterial Cell-Free Systems Engineering. [PDF]

ACS Synth Biol
Lee PW, Maerkl SJ.
europepmc   +1 more source

The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia [PDF]

Journal of Infectious Diseases, 2020
Abstract Staphylococcus aureus is a leading cause of pneumonia. We show here that the ClpXP protease involved in protein turnover is important for pathogenesis in a murine model of acute pneumonia. Staphylococcus aureus lacking this protease is attenuated in vivo, being rapidly cleared from the airway and leading to decreased immune cell
Lavoisier Akoolo, Dane Parker
exaly   +3 more sources

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

Biochimica Et Biophysica Acta - 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
Tania A Baker, Robert T Sauer
exaly   +4 more sources

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A Specificity-Enhancing Factor for the ClpXP Degradation Machine

Science, 2000
Events that stall bacterial protein synthesis activate the ssrA-tagging machinery, resulting in resumption of translation and addition of an 11-residue peptide to the carboxyl terminus of the nascent chain. This ssrA-encoded peptide tag marks the incomplete protein for degradation by the energy-dependent ClpXP protease.
Robert T Sauer, Tania A Baker
exaly   +3 more sources

Discovery of antibacterial cyclic peptides that inhibit the ClpXP protease [PDF]

Protein Science, 2007
AbstractA method to rapidly screen libraries of cyclic peptides in vivo for molecules with biological activity has been developed and used to isolate cyclic peptide inhibitors of the ClpXP protease. Fluorescence activated cell sorting was used in conjunction with a fluorescent reporter to isolate cyclic peptides that inhibit the proteolysis of tmRNA ...
Lin Cheng, Todd A Naumann, Bryan J Venters   +2 more
exaly   +3 more sources

Dynamics of Substrate Denaturation and Translocation by the ClpXP Degradation Machine [PDF]

Molecular Cell, 2000
ClpXP is a protein machine composed of the ClpX ATPase, a member of the Clp/Hsp100 family of remodeling enzymes, and the ClpP peptidase. Here, ClpX and ClpXP are shown to catalyze denaturation of GFP modified with an ssrA degradation tag. ClpX translocates this denatured protein into the proteolytic chamber of ClpP and, when proteolysis is blocked ...
Robert T Sauer, Tania A Baker
exaly   +3 more sources

Alternating translocation of protein substrates from both ends of ClpXP protease [PDF]

EMBO Journal, 2002
In ClpXP protease complexes, hexameric rings of the ATP-dependent ClpX chaperone stack on one or both faces of the double-heptameric rings of ClpP. We used electron microscopy to record the initial binding of protein substrates to ClpXP and their accumulation inside proteolytically inactive ClpP.
Joaquin Ortega
exaly   +3 more sources