http://orcid.org/0000-0001-7041-1655
References
- SauerRTBakerTAAAA+proteases: ATP-fueled machines of protein destructionAnnu. Rev. Biochem201180 587 61210.1146/annurev-biochem-060408-172623
- Torres-CabassaAGottesmanSFrederickRDDolphPJCoplinDLControl of extracellular polysaccharide synthesis in Erwinia stewartii and Escherichia coli K-12: a common regulatory functionJ. Bacteriol.19871694525453110.1128/jb.169.10.4525-4531.1987213817
- JaskolskaMGerdesKCRP-dependent positive autoregulation and proteolytic degradation regulate competence activator Sxy of Escherichia coliMol. Microbiol20159583384510.1111/mmi.12901
- MukherjeeSAdaptor-mediated Lon proteolysis restricts Bacillus subtilis hyperflagellationProc. Natl Acad. Sci. USA201511225025510.1073/pnas.1417419112
- BissonnetteSARivera-RiveraISauerRTBakerTAThe IbpA and IbpB small heat-shock proteins are substrates of the AAA+Lon proteaseMol. Microbiol2010751539154910.1111/j.1365-2958.2010.07070.x3934651
- ShanYATP-dependent persister formation in Escherichia colimBio20178e02267-1610.1128/mBio.02267-165296605
- RicciVBlairJMPiddockLJRamA, which controls expression of the MDR efflux pump AcrAB-TolC, is regulated by the Lon proteaseJ. Antimicrob. Chemother.20146964365010.1093/jac/dkt432
- LeslieDJNutritional control of DNA replication initiation through the proteolysis and regulated translation of DnaAPLoS Genet.201511e100534210.1371/journal.pgen.10053424489657
- JonasKLiuJChienPLaubMTProteotoxic stress induces a cell-cycle arrest by stimulating Lon to degrade the replication initiator DnaACell201315462363610.1016/j.cell.2013.06.0343749246
- HerbstKIntrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovAPLoS Pathog.20095e100043510.1371/journal.ppat.10004352676509
- HeLThe protease locus of Francisella tularensis LVS is required for stress tolerance and infection in the mammalian HostInfect. Immun.2016841387140210.1128/IAI.00076-164862698
- GrallNPivotal role of the Francisella tularensis heat-shock sigma factor RpoHMicrobiology20091552560257210.1099/mic.0.029058-02888120
- WangNMauriziMREmmert-BuckLGottesmanMMSynthesis, processing, and localization of human Lon proteaseJ. Biol. Chem.19942692930829313
- NgoJKDaviesKJMitochondrial Lon protease is a human stress proteinFree Radic. Biol. Med.2009461042104810.1016/j.freeradbiomed.2008.12.0243093304
- MatsushimaYGotoYKaguniLSMitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)Proc. Natl Acad. Sci. USA2010107184101841510.1073/pnas.1008924107
- FukudaRHIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cellsCell200712911112210.1016/j.cell.2007.01.047
- GotoMAdaptation of leukemia cells to hypoxic condition through switching the energy metabolism or avoiding the oxidative stressBMC Cancer20141410.1186/1471-2407-14-763922169
- KitaKSuzukiTOchiTDiphenylarsinic acid promotes degradation of glutaminase C by mitochondrial Lon proteaseJ. Biol. Chem.2012287181631817210.1074/jbc.M112.3626993365764
- KonigJMitochondrial contribution to lipofuscin formationRedox Biol.20171167368110.1016/j.redox.2017.01.0175292761
- PintiMMitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancerCell. Mol. Life Sci.2015724807482410.1007/s00018-015-2039-3
- ChaSSCrystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamberEMBO J.2010293520353010.1038/emboj.2010.2262964173
- KereicheSThe N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon proteaseSci. Rep.2016610.1038/srep336315025710
- WohleverMLBakerTASauerRTRoles of the N domain of the AAA+Lon protease in substrate recognition, allosteric regulation and chaperone activityMol. Microbiol201491667810.1111/mmi.12444
- RotanovaTVSlicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domainsProtein Sci.2006151815182810.1110/ps.0520693062242575
- WohleverMLBakerTASauerRTA mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substratesJ. Bacteriol.20131955622562810.1128/JB.00886-133889616
- KudzhaevAMAndrianovaAGDubovtsevaESSerovaOVRotanovaTVRole of the inserted alpha-helical domain in E. coli ATP-dependent Lon protease functionActa Nat.201797581
- PeterBDefective mitochondrial protease LonP1 can cause classical mitochondrial diseaseHum. Mol. Genet.2018271743175310.1093/hmg/ddy0805932559
- GurEBiranDRonEZRegulated proteolysis in Gram-negative bacteria—how and when?Nat. Rev. Microbiol.2011983984810.1038/nrmicro2669
- LiaoJHBinding and cleavage of E. coli HUβ by the E. coli Lon proteaseBiophys. J.20109812913710.1016/j.bpj.2009.09.0522800966
- StoutVTorres-CabassaAMauriziMRGutnickDGottesmanSRcsA, an unstable positive regulator of capsular polysaccharide synthesisJ. Bacteriol.19911731738174710.1128/jb.173.5.1738-1747.1991207325
- NishiiWCleavage mechanism of ATP-dependent Lon protease toward ribosomal S2 proteinFEBS Lett.20055796846685010.1016/j.febslet.2005.11.026
- ShahIMWolfREJr.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-terminal 21 amino acid residuesJ. Mol. Biol.200635771873110.1016/j.jmb.2005.12.088
- IshiiYRegulatory role of C-terminal residues of SulA in its degradation by Lon protease in Escherichia coliJ. Biochem.200012783784410.1093/oxfordjournals.jbchem.a022677
- BakerTASauerRTATP-dependent proteases of bacteria: recognition logic and operating principlesTrends Biochem. Sci.20063164765310.1016/j.tibs.2006.10.0062717004
- GurESauerRTRecognition of misfolded proteins by Lon, a AAA(+) proteaseGenes Dev.2008222267227710.1101/gad.16709082518814
- GonzalezMFrankEGLevineASWoodgateRLon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysisGenes Dev.1998123889389910.1101/gad.12.24.3889317269
- NishiiWMaruyamaTMatsuokaRMuramatsuTTakahashiKThe unique sites in SulA protein preferentially cleaved by ATP-dependent Lon protease from Escherichia coliEur. J. Biochem.200226945145710.1046/j.0014-2956.2001.02668.x
- ChoyJSAungLLKarzaiAWLon protease degrades transfer-messenger RNA-tagged proteinsJ. Bacteriol.20071896564657110.1128/JB.00860-072045158
- MooreSDSauerRTRibosome rescue: tmRNA tagging activity and capacity in Escherichia coliMol. Microbiol.20055845646610.1111/j.1365-2958.2005.04832.x
- LiesMMauriziMRTurnover of endogenous SsrA-tagged proteins mediated by ATP-dependent proteases in Escherichia coliJ. Biol. Chem.2008283229182292910.1074/jbc.M8016922002516991
- PuriNKarzaiAWHspQ functions as a unique specificity-enhancing factor for the AAA+Lon ProteaseMol. Cell20176667268310.1016/j.molcel.2017.05.016
- HilliardJJSimonLDVan MelderenLMauriziMRPinA inhibits ATP hydrolysis and energy-dependent protein degradation by Lon proteaseJ. Biol. Chem.199827352452710.1074/jbc.273.1.524
- KarlowiczADefining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substratesJ. Biol. Chem.20172927507751810.1074/jbc.M116.7667095418049
- PetersenTNBrunakSvon HeijneGNielsenHSignalP 4.0: discriminating signal peptides from transmembrane regionsNat. Methods2011878578610.1038/nmeth.1701
- EmanuelssonOBrunakSvon HeijneGNielsenHLocating proteins in the cell using TargetP, SignalP and related toolsNat. Protoc.2007295397110.1038/nprot.2007.131
- AntwerpenMHSchachtEKaysserPSplettstoesserWDComplete genome sequence of a Francisella tularensis subsp. holarctica strain from Germany causing lethal infection in common marmosetsGenome Announc.20131e00135-1210.1128/genomeA.00135-123569339
- BaraboteRDComplete genome sequence of Francisella tularensis subspecies holarctica FTNF002-00PLoS ONE20094e704110.1371/journal.pone.00070412737636
- LarssonPThe complete genome sequence of Francisella tularensis, the causative agent of tularemiaNat. Genet.20053715315910.1038/ng1499
- GuerreroJLDaughertyPSO’MalleyMAEmerging technologies for protease engineering: new tools to clear out diseaseBiotechnol. Bioeng.2017114333810.1002/bit.26066
- GriffithKLShahIMWolfREJr.Proteolytic degradation of Escherichia coli transcription activators SoxS and MarA as the mechanism for reversing the induction of the superoxide (SoxRS) and multiple antibiotic resistance (Mar) regulonsMol. Microbiol.2004511801181610.1046/j.1365-2958.2003.03952.x
- SonezakiSOverproduction and purification of SulA fusion protein in Escherichia coli and its degradation by Lon protease in vitroAppl. Microbiol. Biotechnol.19954330430910.1007/BF00172829
- OndrovicovaGCleavage site selection within a folded substrate by the ATP-dependent lon proteaseJ. Biol. Chem.2005280251032511010.1074/jbc.M502796200
- GoldbergALSwamyKChungCHLarimoreFSProteases in Escherichia coliMethods Enzymol.198180PtC68070210.1016/S0076-6879(81)80052-3
- WangNGottesmanSWillinghamMCGottesmanMMMauriziMRA human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon proteaseProc. Natl Acad. Sci. USA199390112471125110.1073/pnas.90.23.11247
- RasulovaFSThe isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activityFEBS Lett.199843217918110.1016/S0014-5793(98)00859-X
- GoardCASchimmerADMitochondrial matrix proteases as novel therapeutic targets in malignancyOncogene2014332690269910.1038/onc.2013.228
- SuJGenome-wide identification of Francisella tularensis virulence determinantsInfect. Immun.2007753089310110.1128/IAI.01865-061932872
- AhnBEBakerTAOxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerRProc. Natl Acad. Sci. USA2016113E23E3110.1073/pnas.1522687112
- AdlerHIHardigreeAAAnalysis of a gene controlling cell division and sensitivity to radiation in Escherichia coliJ. Bacteriol.196487720726277076
- TrentiniDBArginine phosphorylation marks proteins for degradation by a Clp proteaseNature2016539485310.1038/nature20122
- AhlawatSMorrisonDAClpXP degrades SsrA-tagged proteins in Streptococcus pneumoniaeJ. Bacteriol.20091912894289810.1128/JB.01715-082668424
- FinleyDRecognition and processing of ubiquitin-protein conjugates by the proteasomeAnnu. Rev. Biochem.20097847751310.1146/annurev.biochem.78.081507.1016073431160
- ZhouXA phosphorylation switch on Lon protease regulates bacterial type III secretion system in hostMBio20189e02146-1710.1128/mBio.02146-175784255
- NishiiWA redox switch shapes the Lon protease exit pore to facultatively regulate proteolysisNat. Chem. Biol.201511465110.1038/nchembio.1688
- CraikCSPageMJMadisonELProteases as therapeuticsBiochem. J.201143511610.1042/BJ201009654503466
- RenickeCSpadacciniRTaxisCA tobacco etch virus protease with increased substrate tolerance at the P1’ positionPLoS ONE20138e6791510.1371/journal.pone.00679153691164
- YiLEngineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial librariesProc. Natl Acad. Sci. USA20131107229723410.1073/pnas.1215994110
- GuerreroJLO’MalleyMADaughertyPSIntracellular FRET-based screen for redesigning the specificity of secreted proteasesACS Chem. Biol.20161196197010.1021/acschembio.5b01051
- CellaLNBiswasPYatesMVMulchandaniAChenWQuantitative assessment of in vivo HIV protease activity using genetically engineered QD-based FRET probesBiotechnol. Bioeng.20141111082108710.1002/bit.25199
- ChamberlainREEvaluation of live tularemia vaccine prepared in a chemically defined mediumAppl. Microbiol1965132322351058227
- LiuZSilencing PRDX3 inhibits growth and promotes invasion and extracellular matrix degradation in hepatocellular carcinoma cellsJ. Proteome Res.2016151506151410.1021/acs.jproteome.5b01125
- FengJTrapping and proteomic identification of cellular substrates of the ClpP protease in Staphylococcus aureusJ. Proteome Res.20131254755810.1021/pr300394r
- LoVulloEDMillerCNPavelkaMSJr.KawulaTHTetR-based gene regulation systems for Francisella tularensisAppl. Environ. Microbiol.2012786883688910.1128/AEM.01679-123457491
- SuJThe capBCA locus is required for intracellular growth of Francisella tularensis LVSFront. Microbiol.20112833128946
- PenaIDominguezJMThermally denatured BSA, a surrogate additive to replace BSA in buffers for high-throughput screeningJ. Biomol. Screen.2010151281128610.1177/1087057110379768
- JinLDown-regulation of Ras-related protein Rab 5C-dependent endocytosis and glycolysis in cisplatin-resistant ovarian cancer cell linesMol. Cell. Proteomics2014133138315110.1074/mcp.M113.0332174223497
- GreenfieldNJUsing circular dichroism spectra to estimate protein secondary structureNat. Protoc.200612876289010.1038/nprot.2006.2022728378
- ThomsenMCNielsenMSeq2Logo: a method for construction and visualization of amino acid binding motifs and sequence profiles including sequence weighting, pseudo counts and two-sided representation of amino acid enrichment and depletionNucleic Acids Res.201240W281W28710.1093/nar/gks4693394285