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Volumn 114, Issue 6, 2017, Pages 1311-1316

Mechanism of catalysis, E2 recognition,& autoinhibition for the IpaH family of bacterial E3 ubiquitin ligases

Author keywords

Bacterial E3 ubiquitin ligase; Host pathogen; IpaH family; Ubiquitin

Indexed keywords

CYSTEINE; UBIQUITIN PROTEIN LIGASE E3; BACTERIAL PROTEIN; RECOMBINANT PROTEIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

EID: 85011636010     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1611595114     Document Type: Article
Times cited : (26)

References (51)
  • 1
    • 84861877407 scopus 로고    scopus 로고
    • The ubiquitin code
    • Komander D, Rape M (2012) The ubiquitin code. Annu Rev Biochem 81(1):203-229.
    • (2012) Annu Rev Biochem , vol.81 , Issue.1 , pp. 203-229
    • Komander, D.1    Rape, M.2
  • 2
    • 84971236561 scopus 로고    scopus 로고
    • The increasing complexity of the ubiquitin code
    • Yau R, Rape M (2016) The increasing complexity of the ubiquitin code. Nat Cell Biol 18(6):579-586.
    • (2016) Nat Cell Biol , vol.18 , Issue.6 , pp. 579-586
    • Yau, R.1    Rape, M.2
  • 3
    • 84866858702 scopus 로고    scopus 로고
    • Structure of an E3:E2∼Ub complex reveals an allosteric mechanism shared among RING/U-box ligases
    • Pruneda JN, et al. (2012) Structure of an E3:E2∼Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. Mol Cell 47(6):933-942.
    • (2012) Mol Cell , vol.47 , Issue.6 , pp. 933-942
    • Pruneda, J.N.1
  • 4
    • 84901988917 scopus 로고    scopus 로고
    • Structural and functional insights to ubiquitin-like protein conjugation
    • Streich FC Jr, Lima CD (2014) Structural and functional insights to ubiquitin-like protein conjugation. Annu Rev Biophys 43:357-379.
    • (2014) Annu Rev Biophys , vol.43 , pp. 357-379
    • Streich, F.C.1    Lima, C.D.2
  • 5
    • 84898754901 scopus 로고    scopus 로고
    • New insights into ubiquitin E3 ligase mechanism
    • Berndsen CE, Wolberger C (2014) New insights into ubiquitin E3 ligase mechanism. Nat Struct Mol Biol 21(4):301-307.
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.4 , pp. 301-307
    • Berndsen, C.E.1    Wolberger, C.2
  • 6
    • 84922393807 scopus 로고    scopus 로고
    • Ubiquitination in disease pathogenesis and treatment
    • Popovic D, Vucic D, Dikic I (2014) Ubiquitination in disease pathogenesis and treatment. Nat Med 20(11):1242-1253.
    • (2014) Nat Med , vol.20 , Issue.11 , pp. 1242-1253
    • Popovic, D.1    Vucic, D.2    Dikic, I.3
  • 7
    • 84928203901 scopus 로고    scopus 로고
    • Activation of a primed RING E3-E2-ubiquitin complex by noncovalent ubiquitin
    • Buetow L, et al. (2015) Activation of a primed RING E3-E2-ubiquitin complex by noncovalent ubiquitin. Mol Cell 58(2):297-310.
    • (2015) Mol Cell , vol.58 , Issue.2 , pp. 297-310
    • Buetow, L.1
  • 9
    • 84906859924 scopus 로고    scopus 로고
    • Sumoylation controls host anti-bacterial response to the gut invasive pathogen Shigella flexneri
    • Fritah S, et al. (2014) Sumoylation controls host anti-bacterial response to the gut invasive pathogen Shigella flexneri. EMBO Rep 15(9):965-972.
    • (2014) EMBO Rep , vol.15 , Issue.9 , pp. 965-972
    • Fritah, S.1
  • 10
    • 84918775747 scopus 로고    scopus 로고
    • The bacterial pathogen-ubiquitin interface: Lessons learned from Shigella
    • Tanner K, Brzovic P, Rohde JR (2015) The bacterial pathogen-ubiquitin interface: Lessons learned from Shigella. Cell Microbiol 17(1):35-44.
    • (2015) Cell Microbiol , vol.17 , Issue.1 , pp. 35-44
    • Tanner, K.1    Brzovic, P.2    Rohde, J.R.3
  • 11
    • 84902332058 scopus 로고    scopus 로고
    • Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG
    • Grishin AM, et al. (2014) Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG. Structure 22(6):878-888.
    • (2014) Structure , vol.22 , Issue.6 , pp. 878-888
    • Grishin, A.M.1
  • 12
    • 84898660353 scopus 로고    scopus 로고
    • E2∼Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis
    • Pruneda JN, et al. (2014) E2∼Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis. EMBO J 33(5):437-449.
    • (2014) EMBO J , vol.33 , Issue.5 , pp. 437-449
    • Pruneda, J.N.1
  • 13
    • 84862818454 scopus 로고    scopus 로고
    • The Shigella flexneri effector OspI deamidates UBC13 to dampen the inflammatory response
    • Sanada T, et al. (2012) The Shigella flexneri effector OspI deamidates UBC13 to dampen the inflammatory response. Nature 483(7391):623-626.
    • (2012) Nature , vol.483 , Issue.7391 , pp. 623-626
    • Sanada, T.1
  • 14
    • 84855764312 scopus 로고    scopus 로고
    • Cysteine methylation disrupts ubiquitin-chain sensing in NF-κB activation
    • Zhang L, et al. (2011) Cysteine methylation disrupts ubiquitin-chain sensing in NF-κB activation. Nature 481(7380):204-208.
    • (2011) Nature , vol.481 , Issue.7380 , pp. 204-208
    • Zhang, L.1
  • 15
    • 37849010910 scopus 로고    scopus 로고
    • Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase
    • Diao J, Zhang Y, Huibregtse JM, Zhou D, Chen J (2008) Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase. Nat Struct Mol Biol 15(1):65-70.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.1 , pp. 65-70
    • Diao, J.1    Zhang, Y.2    Huibregtse, J.M.3    Zhou, D.4    Chen, J.5
  • 16
    • 30844458212 scopus 로고    scopus 로고
    • A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase
    • Janjusevic R, Abramovitch RB, Martin GB, Stebbins CE (2006) A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science 311(5758): 222-226.
    • (2006) Science , vol.311 , Issue.5758 , pp. 222-226
    • Janjusevic, R.1    Abramovitch, R.B.2    Martin, G.B.3    Stebbins, C.E.4
  • 18
    • 85006230740 scopus 로고    scopus 로고
    • Shigella IpaH family effectors as a versatile model for studying pathogenic bacteria
    • Ashida H, Sasakawa C (2016) Shigella IpaH family effectors as a versatile model for studying pathogenic bacteria. Front Cell Infect Microbiol 5:100.
    • (2016) Front Cell Infect Microbiol , vol.5 , pp. 100
    • Ashida, H.1    Sasakawa, C.2
  • 19
    • 84908424472 scopus 로고    scopus 로고
    • Shigella IpaH7.8 E3 ubiquitin ligase targets glomulin and activates inflammasomes to demolish macrophages
    • Suzuki S, et al. (2014) Shigella IpaH7.8 E3 ubiquitin ligase targets glomulin and activates inflammasomes to demolish macrophages. Proc Natl Acad Sci USA 111(40): E4254-E4263.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.40 , pp. E4254-E4263
    • Suzuki, S.1
  • 20
    • 77955109451 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response
    • 1-9
    • Ashida H, et al. (2010) A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat Cell Biol 12(1): 66-73, 1-9.
    • (2010) Nat Cell Biol , vol.12 , Issue.1 , pp. 66-73
    • Ashida, H.1
  • 21
    • 57149098210 scopus 로고    scopus 로고
    • Structure of a Shigella effector reveals a new class of ubiquitin ligases
    • Zhu Y, et al. (2008) Structure of a Shigella effector reveals a new class of ubiquitin ligases. Nat Struct Mol Biol 15(12):1302-1308.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.12 , pp. 1302-1308
    • Zhu, Y.1
  • 22
    • 57149105701 scopus 로고    scopus 로고
    • Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
    • Singer AU, et al. (2008) Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases. Nat Struct Mol Biol 15(12):1293-1301.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.12 , pp. 1293-1301
    • Singer, A.U.1
  • 23
    • 63849280748 scopus 로고    scopus 로고
    • A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases
    • Quezada CM, Hicks SW, Galán JE, Stebbins CE (2009) A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases. Proc Natl Acad Sci USA 106(12):4864-4869.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.12 , pp. 4864-4869
    • Quezada, C.M.1    Hicks, S.W.2    Galán, J.E.3    Stebbins, C.E.4
  • 24
    • 84855287935 scopus 로고    scopus 로고
    • Conserved structural mechanisms for autoinhibition in IpaH ubiquitin ligases
    • Chou Y-C, Keszei AFA, Rohde JR, Tyers M, Sicheri F (2012) Conserved structural mechanisms for autoinhibition in IpaH ubiquitin ligases. J Biol Chem 287(1):268-275.
    • (2012) J Biol Chem , vol.287 , Issue.1 , pp. 268-275
    • Chou, Y.-C.1    Keszei, A.F.A.2    Rohde, J.R.3    Tyers, M.4    Sicheri, F.5
  • 25
    • 84892473685 scopus 로고    scopus 로고
    • Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase
    • Keszei AFA, et al. (2014) Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol 34(3):362-373.
    • (2014) Mol Cell Biol , vol.34 , Issue.3 , pp. 362-373
    • Keszei, A.F.A.1
  • 26
    • 84908365192 scopus 로고    scopus 로고
    • The structure of the Slrp-Trx1 complex sheds light on the autoinhibition mechanism of the type III secretion system effectors of the NEL family
    • Zouhir S, et al. (2014) The structure of the Slrp-Trx1 complex sheds light on the autoinhibition mechanism of the type III secretion system effectors of the NEL family. Biochem J 464(1):135-144.
    • (2014) Biochem J , vol.464 , Issue.1 , pp. 135-144
    • Zouhir, S.1
  • 27
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovová A, Jaffray EG, Tatham MH, Naismith JH, Hay RT (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489(7414): 115-120.
    • (2012) Nature , vol.489 , Issue.7414 , pp. 115-120
    • Plechanovova, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 28
    • 84866124869 scopus 로고    scopus 로고
    • BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
    • Dou H, Buetow L, Sibbet GJ, Cameron K, Huang DT (2012) BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat Struct Mol Biol 19(9):876-883.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.9 , pp. 876-883
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3    Cameron, K.4    Huang, D.T.5
  • 29
    • 84881518558 scopus 로고    scopus 로고
    • Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
    • Kamadurai HB, et al. (2013) Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3. eLife 2:e00828.
    • (2013) ELife , vol.2 , pp. e00828
    • Kamadurai, H.B.1
  • 30
    • 84888034624 scopus 로고    scopus 로고
    • Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP
    • Stieglitz B, et al. (2013) Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP. Nature 503(7476):422-426.
    • (2013) Nature , vol.503 , Issue.7476 , pp. 422-426
    • Stieglitz, B.1
  • 31
    • 84881478295 scopus 로고    scopus 로고
    • Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3
    • Dou H, Buetow L, Sibbet GJ, Cameron K, Huang DT (2013) Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3. Nat Struct Mol Biol 20(8):982-986.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.8 , pp. 982-986
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3    Cameron, K.4    Huang, D.T.5
  • 32
    • 72149107116 scopus 로고    scopus 로고
    • Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECTNEDD4L complex
    • Kamadurai HB, et al. (2009) Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECTNEDD4L complex. Mol Cell 36(6):1095-1102.
    • (2009) Mol Cell , vol.36 , Issue.6 , pp. 1095-1102
    • Kamadurai, H.B.1
  • 33
    • 34547958577 scopus 로고    scopus 로고
    • Autoinhibition of the HECT-Type ubiquitin ligase Smurf2 through its C2 domain
    • Wiesner S, et al. (2007) Autoinhibition of the HECT-Type ubiquitin ligase Smurf2 through its C2 domain. Cell 130(4):651-662.
    • (2007) Cell , vol.130 , Issue.4 , pp. 651-662
    • Wiesner, S.1
  • 34
    • 84908510945 scopus 로고    scopus 로고
    • Structural and functional framework for the autoinhibition of Nedd4-family ubiquitin ligases
    • Mari S, et al. (2014) Structural and functional framework for the autoinhibition of Nedd4-family ubiquitin ligases. Structure 22(11):1639-1649.
    • (2014) Structure , vol.22 , Issue.11 , pp. 1639-1649
    • Mari, S.1
  • 35
    • 84965040841 scopus 로고    scopus 로고
    • World Health Organization, World Health Organization, Geveva, Switzerland
    • World Health Organization (2014) Antimicrobial Resistance: Global Report on Surveillance (World Health Organization, Geveva, Switzerland).
    • (2014) Antimicrobial Resistance: Global Report on Surveillance
  • 37
    • 84893786916 scopus 로고    scopus 로고
    • Targeting virulence: Can we make evolution-proof drugs?
    • Allen RC, Popat R, Diggle SP, Brown SP (2014) Targeting virulence: Can we make evolution-proof drugs? Nat Rev Microbiol 12(4):300-308.
    • (2014) Nat Rev Microbiol , vol.12 , Issue.4 , pp. 300-308
    • Allen, R.C.1    Popat, R.2    Diggle, S.P.3    Brown, S.P.4
  • 38
    • 84978208848 scopus 로고    scopus 로고
    • Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms
    • Dove KK, Stieglitz B, Duncan ED, Rittinger K, Klevit RE (2016) Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms. EMBO Rep 17(8):1221-1235.
    • (2016) EMBO Rep , vol.17 , Issue.8 , pp. 1221-1235
    • Dove, K.K.1    Stieglitz, B.2    Duncan, E.D.3    Rittinger, K.4    Klevit, R.E.5
  • 39
    • 84956664551 scopus 로고    scopus 로고
    • Structure of a HOIP/E2∼ubiquitin complex reveals RBR E3 ligase mechanism and regulation
    • Lechtenberg BC, et al. (2016) Structure of a HOIP/E2∼ubiquitin complex reveals RBR E3 ligase mechanism and regulation. Nature 529(7587):546-550.
    • (2016) Nature , vol.529 , Issue.7587 , pp. 546-550
    • Lechtenberg, B.C.1
  • 40
    • 84878900697 scopus 로고    scopus 로고
    • Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming
    • Maspero E, et al. (2013) Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming. Nat Struct Mol Biol 20(6):696-701.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.6 , pp. 696-701
    • Maspero, E.1
  • 41
    • 77649242746 scopus 로고    scopus 로고
    • Identification of an unconventional E3 binding surface on the UbcH5∼Ub conjugate recognized by a pathogenic bacterial E3 ligase
    • Levin I, et al. (2010) Identification of an unconventional E3 binding surface on the UbcH5∼Ub conjugate recognized by a pathogenic bacterial E3 ligase. Proc Natl Acad Sci USA 107(7):2848-2853.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.7 , pp. 2848-2853
    • Levin, I.1
  • 42
    • 0034117282 scopus 로고    scopus 로고
    • Nedd8 modification of cul-1 activates SCF(beta(TrCP))- dependent ubiquitination of IkappaBalpha
    • Read MA, et al. (2000) Nedd8 modification of cul-1 activates SCF(beta(TrCP))- dependent ubiquitination of IkappaBalpha. Mol Cell Biol 20(7):2326-2333.
    • (2000) Mol Cell Biol , vol.20 , Issue.7 , pp. 2326-2333
    • Read, M.A.1
  • 43
    • 84878840303 scopus 로고    scopus 로고
    • Structure of HHARI, a RING-IBR-RING ubiquitin ligase: Autoinhibition of an Ariadne-family E3 and insights into ligation mechanism
    • Duda DM, et al. (2013) Structure of HHARI, a RING-IBR-RING ubiquitin ligase: Autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure 21(6):1030-1041.
    • (2013) Structure , vol.21 , Issue.6 , pp. 1030-1041
    • Duda, D.M.1
  • 44
    • 84892678766 scopus 로고    scopus 로고
    • Bacteria-Autophagy interplay: A battle for survival
    • Huang J, Brumell JH (2014) Bacteria-Autophagy interplay: A battle for survival. Nat Rev Microbiol 12(2):101-114.
    • (2014) Nat Rev Microbiol , vol.12 , Issue.2 , pp. 101-114
    • Huang, J.1    Brumell, J.H.2
  • 45
    • 0035943712 scopus 로고    scopus 로고
    • Shigella protein IpaH(9.8) is secreted from bacteria within mammalian cells and transported to the nucleus
    • Toyotome T, et al. (2001) Shigella protein IpaH(9.8) is secreted from bacteria within mammalian cells and transported to the nucleus. J Biol Chem 276(34):32071-32079.
    • (2001) J Biol Chem , vol.276 , Issue.34 , pp. 32071-32079
    • Toyotome, T.1
  • 46
    • 0037972467 scopus 로고    scopus 로고
    • A Salmonella enterica serovar typhimurium translocated leucine-rich repeat effector protein inhibits NF-κ B-dependent gene expression
    • Haraga A, Miller SI (2003) A Salmonella enterica serovar typhimurium translocated leucine-rich repeat effector protein inhibits NF-κ B-dependent gene expression. Infect Immun 71(7):4052-4058.
    • (2003) Infect Immun , vol.71 , Issue.7 , pp. 4052-4058
    • Haraga, A.1    Miller, S.I.2
  • 47
    • 84896639811 scopus 로고    scopus 로고
    • E2 enzyme inhibition by stabilization of a low-Affinity interface with ubiquitin
    • Huang H, et al. (2014) E2 enzyme inhibition by stabilization of a low-Affinity interface with ubiquitin. Nat Chem Biol 10(2):156-163.
    • (2014) Nat Chem Biol , vol.10 , Issue.2 , pp. 156-163
    • Huang, H.1
  • 48
    • 23044505285 scopus 로고    scopus 로고
    • Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain
    • Ogunjimi AA, et al. (2005) Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain. Mol Cell 19(3):297-308.
    • (2005) Mol Cell , vol.19 , Issue.3 , pp. 297-308
    • Ogunjimi, A.A.1
  • 49
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments
    • Bond CS, Schüttelkopf AW (2009) ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr D Biol Crystallogr 65(Pt 5): 510-512.
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , pp. 510-512
    • Bond, C.S.1    Schüttelkopf, A.W.2
  • 50
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F, et al. (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7:539.
    • (2011) Mol Syst Biol , vol.7 , pp. 539
    • Sievers, F.1
  • 51
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera: A visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1


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