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Original Articles

Acetylation of lysine 182 inhibits the ability of Mycobacterium tuberculosis DosR to bind DNA and regulate gene expression during hypoxia

, ORCID Icon, , , , , & show all
Pages 1-12 | Received 08 Mar 2018, Accepted 16 May 2018, Published online: 13 Jun 2018

References

  • The World Health Organization. Global tuberculosis report 2016 (2016).
  • NorthRJJungYJImmunity to tuberculosisAnnu. Rev. Immunol.200422 599 62310.1146/annurev.immunol.22.012703.104635
  • StewartGRRobertsonBDYoungDBTuberculosis: a problem with persistenceNat. Rev. Microbiol.200319710.1038/nrmicro749
  • ChaoMCRubinEJLetting sleeping dos lie: does dormancy play a role in tuberculosis?Annu. Rev. Microbiol20106429331110.1146/annurev.micro.112408.134043
  • WayneLGSohaskeyCDNonreplicating persistence of Mycobacterium tuberculosisAnnu. Rev. Microbiol20015513916310.1146/annurev.micro.55.1.139
  • BoonCDickTMycobacterium bovis BCG response regulator essential for hypoxic dormancyJ. Bacteriol.20021846760676710.1128/JB.184.24.6760-6767.2002135468
  • DasguptaNCharacterization of a two-component system, devR-devS, of Mycobacterium tuberculosisTuber. Lung Dis.20008014115910.1054/tuld.2000.0240
  • ParkHDRv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosisMol. Microbiol.20034883384310.1046/j.1365-2958.2003.03474.x1992516
  • BretlDJDemetriadouCZahrtTCAdaptation to environmental stimuli within the host: two-component signal transduction systems of Mycobacterium tuberculosisMicrobiol. Mol. Biol. Rev.20117556658210.1128/MMBR.05004-113232741
  • KendallSThe Mycobacterium tuberculosis dosRS two-component system is induced by multiple stressesTuberculosis20048424725510.1016/j.tube.2003.12.007
  • VoskuilMIInhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy programJ. Exp. Med.200319870571310.1084/jem.200302052194188
  • KumarAToledoJCPatelRPLancasterJRSteynAJMycobacterium tuberculosis DosS is a redox sensor and DosT is a hypoxia sensorProc. Natl Acad. Sci. USA2007104115681157310.1073/pnas.07050541041906723
  • HonakerRWLeistikowRLBartekILVoskuilMIUnique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancyInfect. Immun.2009773258326310.1128/IAI.01449-082715697
  • RobertsDMLiaoRPWisedchaisriGHolWGShermanDRTwo sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosisJ. Biol. Chem.2004279230822308710.1074/jbc.M4012302001458500
  • ShermanDRRegulation of the Mycobacterium tuberculosis hypoxic response gene encoding α-crystallinProc. Natl Acad. Sci. USA2001987534753910.1073/pnas.12117249834703
  • GautamUSSikriKVashistASinghVTyagiJSEssentiality of DevR/DosR interaction with SigA for the dormancy survival program in Mycobacterium tuberculosisJ. Bacteriol.201419679079910.1128/JB.01270-133911168
  • SivaramakrishnanSOrtiz de MontellanoPRThe DosS-DosT/DosR mycobacterial sensor systemBiosensors2013325928210.3390/bios30302594082495
  • SainiDKDevR–DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevRMicrobiology200415086587510.1099/mic.0.26218-0
  • WisedchaisriGWuMShermanDRHolWGCrystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activationJ. Mol. Biol.200837822724210.1016/j.jmb.2008.02.0292364609
  • WisedchaisriGStructures of Mycobacterium tuberculosis DosR and DosR–DNA complex involved in gene activation during adaptation to hypoxic latencyJ. Mol. Biol.200535463064110.1016/j.jmb.2005.09.048
  • ChauhanSTyagiJSCooperative binding of phosphorylated DevR to upstream sites is necessary and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium tuberculosis: implication in the induction of DevR target genesJ. Bacteriol.20081904301431210.1128/JB.01308-072446764
  • MinchKRustadTShermanDRMycobacterium tuberculosis growth following aerobic expression of the DosR regulonPLoS ONE20127e3593510.1371/journal.pone.00359353338750
  • Flores-ValdezMAOverexpression of DosR in Mycobacterium tuberculosis does not affect aerobic replication in vitro or in murine macrophagesAnn. Microbiol20156571372010.1007/s13213-014-0910-3
  • RenJAcetylation of lysine 201 inhibits the DNA-binding ability of PhoP to regulate Salmonella virulencePLoS Pathog.201612e100545810.1371/journal.ppat.10054584778762
  • HuLIAcetylation of the response regulator RcsB controls transcription from a small RNA promoterJ. Bacteriol.20131954174418610.1128/JB.00383-133754749
  • LiRCobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheYMol. Microbiol.2010761162117410.1111/j.1365-2958.2010.07125.x2883070
  • SangYProtein acetylation is involved in Salmonella enterica serovar Typhimurium virulenceJ. Infect. Dis.20162131836184510.1093/infdis/jiw028
  • SangYAcetylation regulating protein stability and DNA-binding ability of HilD, thus modulating Salmonella typhimurium virulenceJ. Infect. Dis.20172161018102610.1093/infdis/jix102
  • Castaño‐CerezoSProtein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coliMol. Syst. Biol.20141076210.15252/msb.201452274299603
  • BiJModulation of central carbon metabolism by acetylation of isocitrate lyase in Mycobacterium tuberculosisSci. Rep.2017710.1038/srep448265359664
  • LiuFAcetylome analysis reveals diverse functions of lysine acetylation in Mycobacterium tuberculosisMol. Cell. Proteomics2014133352336610.1074/mcp.M114.0419624256489
  • GuptaRKChauhanSTyagiJSK182G substitution in DevR or C8G mutation in the Dev box impairs protein–DNA interaction and abrogates DevR‐mediated gene induction in Mycobacterium tuberculosisFEBS J.20112782131213910.1111/j.1742-4658.2011.08130.x
  • GuptaRKThakurTSDesirajuGRTyagiJSStructure-based design of DevR inhibitor active against nonreplicating Mycobacterium tuberculosisJ. Med. Chem.2009526324633410.1021/jm900358q
  • HuLILimaBPWolfeAJBacterial protein acetylation: the dawning of a new ageMol. Microbiol.201077152110.1111/j.1365-2958.2010.07204.x2907427
  • NeumannHPeak-ChewSYChinJWGenetically encoding Nε-acetyllysine in recombinant proteinsNat. Chem. Biol.2008423223410.1038/nchembio.73
  • GuJCloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosisBiochemistry (Mosc.)20097474374810.1134/S0006297909070062
  • YangHLysine acetylation of DosR regulates the hypoxia response of Mycobacterium tuberculosisEmerg. Microbes Infect.201873410.1038/s41426-018-0032-25861037
  • RenJSangYLuJYaoYFProtein acetylation and its role in bacterial virulenceTrends Microbiol.20172576877910.1016/j.tim.2017.04.001
  • BagchiGChauhanSSharmaDTyagiJSTranscription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosisMicrobiology20051514045405310.1099/mic.0.28333-0
  • McDermottWTompsettRActivation of pyrazinamide and nicotinamide in acidic environments in vitroAm. Rev. Tuberc.195470748754
  • MackanessGThe intracellular activation of pyrazinamide and nicotinamideAm. Rev. Tuberc.195674718728
  • MurrayMFNicotinamide: an oral antimicrobial agent with activity against both Mycobacterium tuberculosis and human immunodeficiency virusClin. Infect. Dis.20033645346010.1086/367544
  • MarksPARichonVMMillerTKellyWKHistone deacetylase inhibitorsAdv. Cancer Res.20049113716810.1016/S0065-230X(04)91004-4
  • ColeSDeciphering the biology of Mycobacterium tuberculosis from the complete genome sequenceNature199839353710.1038/31159
  • Benjak, A., Sala, C. & Hartkoorn, R. C. in Mycobacteria Protocols (eds Parish, T. & Roberts, D. M.) (Ch. 2) (Humana Press Inc., New York, NY, USA, 2015)