Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-ter

Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-ter

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http://www.wikidata.org/entity/Q33233198

Q33233198

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Multitasking in the mitochondrion by the ATP-dependent Lon protease Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and independent transcriptional networks Intrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA.The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.Recognition of misfolded proteins by Lon, a AAA(+) protease A mixed incoherent feed-forward loop allows conditional regulation of response dynamics.Dialogue between E. coli free radical pathways and the mitochondria of C. elegans.Oxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerR.ATP-dependent proteases of bacteria: recognition logic and operating principles The Protease Locus of Francisella tularensis LVS Is Required for Stress Tolerance and Infection in the Mammalian Host.Two functions of the C-terminal domain of Escherichia coli Rob: mediating "sequestration-dispersal" as a novel off-on switch for regulating Rob's activity as a transcription activator and preventing degradation of Rob by Lon protease.Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine.Proteolysis in the Escherichia coli heat shock response: a player at many levels.Mini review: ATP-dependent proteases in bacteria.Conditional Proteolysis of the Membrane Protein YfgM by the FtsH Protease Depends on a Novel N-terminal Degron.Regulated proteolysis of a transcription factor complex is critical to cell cycle progression in Caulobacter crescentus.A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.The Copper Efflux Regulator CueR Is Subject to ATP-Dependent Proteolysis in Escherichia coli.RamA, which controls expression of the MDR efflux pump AcrAB-TolC, is regulated by the Lon protease Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR Quality control of a molybdoenzyme by the Lon protease.Polyphosphate Kinase Antagonizes Virulence Gene Expression in Francisella tularensis.In vivo trapping of FtsH substrates by label-free quantitative proteomics.Termination of Vibrio cholerae virulence gene expression is mediated by proteolysis of the major virulence activator, ToxT Multiple domains of bacterial and human Lon proteases define substrate selectivity

P2860

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P2860

Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-ter

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http://www.wikidata.org/entity/Q33233198

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