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Volumn 112, Issue 45, 2015, Pages 13862-13867

Defining the mRNA recognition signature of a bacterial toxin protein

Author keywords

Protein synthesis; Ribosome; RNases; Stringent response; Toxin antitoxin systems

Indexed keywords

ADENOSINE; BACTERIAL PROTEIN; BACTERIAL RNA; BACTERIAL TOXIN; CYTOSINE; HIGB TOXIN; MESSENGER RNA; NUCLEOTIDE; RIBONUCLEASE; TRANSFER RNA; UNCLASSIFIED DRUG; CODON;

EID: 84946944535     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1512959112     Document Type: Article
Times cited : (27)

References (51)
  • 1
    • 84899505083 scopus 로고    scopus 로고
    • Molecular mechanisms underlying bacterial persisters
    • Maisonneuve E, Gerdes K (2014) Molecular mechanisms underlying bacterial persisters. Cell 157(3):539-548.
    • (2014) Cell , vol.157 , Issue.3 , pp. 539-548
    • Maisonneuve, E.1    Gerdes, K.2
  • 2
    • 84875852284 scopus 로고    scopus 로고
    • Bacterial lifestyle shapes stringent response activation
    • Boutte CC, Crosson S (2013) Bacterial lifestyle shapes stringent response activation. Trends Microbiol 21(4):174-180.
    • (2013) Trends Microbiol , vol.21 , Issue.4 , pp. 174-180
    • Boutte, C.C.1    Crosson, S.2
  • 4
    • 18044367581 scopus 로고    scopus 로고
    • PpGpp: A global regulator in Escherichia coli
    • Magnusson LU, Farewell A, Nyström T (2005) ppGpp: A global regulator in Escherichia coli. Trends Microbiol 13(5):236-242.
    • (2005) Trends Microbiol , vol.13 , Issue.5 , pp. 236-242
    • Magnusson, L.U.1    Farewell, A.2    Nyström, T.3
  • 5
    • 67049145664 scopus 로고    scopus 로고
    • The chromosomal toxin gene yafQ is a determinant of multidrug tolerance for Escherichia coli growing in a biofilm
    • Harrison JJ, et al. (2009) The chromosomal toxin gene yafQ is a determinant of multidrug tolerance for Escherichia coli growing in a biofilm. Antimicrob Agents Chemother 53(6):2253-2258.
    • (2009) Antimicrob Agents Chemother , vol.53 , Issue.6 , pp. 2253-2258
    • Harrison, J.J.1
  • 6
    • 72949116993 scopus 로고    scopus 로고
    • Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli
    • Kim Y, Wood TK (2010) Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli. Biochem Biophys Res Commun 391(1):209-213.
    • (2010) Biochem Biophys Res Commun , vol.391 , Issue.1 , pp. 209-213
    • Kim, Y.1    Wood, T.K.2
  • 8
    • 84883342218 scopus 로고    scopus 로고
    • (p)ppGpp controls bacterial persistence by stochastic induction of toxin-antitoxin activity
    • Maisonneuve E, Castro-Camargo M, Gerdes K (2013) (p)ppGpp controls bacterial persistence by stochastic induction of toxin-antitoxin activity. Cell 154(5):1140-1150.
    • (2013) Cell , vol.154 , Issue.5 , pp. 1140-1150
    • Maisonneuve, E.1    Castro-Camargo, M.2    Gerdes, K.3
  • 9
    • 84868113986 scopus 로고    scopus 로고
    • Toxin-antitoxin systems are important for niche-specific colonization and stress resistance of uropathogenic Escherichia coli
    • Norton JP, Mulvey MA (2012) Toxin-antitoxin systems are important for niche-specific colonization and stress resistance of uropathogenic Escherichia coli. PLoS Pathog 8(10):e1002954.
    • (2012) PLoS Pathog , vol.8 , Issue.10 , pp. e1002954
    • Norton, J.P.1    Mulvey, M.A.2
  • 10
    • 80052611381 scopus 로고    scopus 로고
    • Toxin-antitoxin systems influence biofilm and persister cell formation and the general stress response
    • Wang X, Wood TK (2011) Toxin-antitoxin systems influence biofilm and persister cell formation and the general stress response. Appl Environ Microbiol 77(16):5577-5583.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.16 , pp. 5577-5583
    • Wang, X.1    Wood, T.K.2
  • 11
    • 84892181925 scopus 로고    scopus 로고
    • Internalization of Salmonella by macrophages induces formation of nonreplicating persisters
    • Helaine S, et al. (2014) Internalization of Salmonella by macrophages induces formation of nonreplicating persisters. Science 343(6167):204-208.
    • (2014) Science , vol.343 , Issue.6167 , pp. 204-208
    • Helaine, S.1
  • 13
    • 0026728290 scopus 로고
    • Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes
    • Bernard P, Couturier M (1992) Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes. J Mol Biol 226(3):735-745.
    • (1992) J Mol Biol , vol.226 , Issue.3 , pp. 735-745
    • Bernard, P.1    Couturier, M.2
  • 14
    • 80053563668 scopus 로고    scopus 로고
    • Selective translation of leaderless mRNAs by specialized ribo-somes generated by MazF in Escherichia coli
    • Vesper O, et al. (2011) Selective translation of leaderless mRNAs by specialized ribo-somes generated by MazF in Escherichia coli. Cell 147(1):147-157.
    • (2011) Cell , vol.147 , Issue.1 , pp. 147-157
    • Vesper, O.1
  • 15
    • 79956328889 scopus 로고    scopus 로고
    • Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA
    • Winther KS, Gerdes K (2011) Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA. Proc Natl Acad Sci USA 108(18):7403-7407.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.18 , pp. 7403-7407
    • Winther, K.S.1    Gerdes, K.2
  • 16
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
    • Pedersen K, et al. (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112(1):131-140.
    • (2003) Cell , vol.112 , Issue.1 , pp. 131-140
    • Pedersen, K.1
  • 17
    • 0242361323 scopus 로고    scopus 로고
    • MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli
    • Zhang Y, et al. (2003) MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol Cell 12(4):913-923.
    • (2003) Mol Cell , vol.12 , Issue.4 , pp. 913-923
    • Zhang, Y.1
  • 18
    • 84887997250 scopus 로고    scopus 로고
    • The Fic protein Doc uses an inverted substrate to phos-phorylate and inactivate EF-Tu
    • Castro-Roa D, et al. (2013) The Fic protein Doc uses an inverted substrate to phos-phorylate and inactivate EF-Tu. Nat Chem Biol 9(12):811-817.
    • (2013) Nat Chem Biol , vol.9 , Issue.12 , pp. 811-817
    • Castro-Roa, D.1
  • 19
    • 84890639139 scopus 로고    scopus 로고
    • HipA-mediated antibiotic persistence via phosphorylation of the glutamyl-tRNA-synthetase
    • Kaspy I, et al. (2013) HipA-mediated antibiotic persistence via phosphorylation of the glutamyl-tRNA-synthetase. Nat Commun 4:3001.
    • (2013) Nat Commun , vol.4 , pp. 3001
    • Kaspy, I.1
  • 20
    • 84878149208 scopus 로고    scopus 로고
    • Mycobacterial toxin MazF-mt6 inhibits translation through cleavage of 23S rRNA at the ribosomal A site
    • Schifano JM, et al. (2013) Mycobacterial toxin MazF-mt6 inhibits translation through cleavage of 23S rRNA at the ribosomal A site. Proc Natl Acad Sci USA 110(21): 8501-8506.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.21 , pp. 8501-8506
    • Schifano, J.M.1
  • 21
    • 71149087505 scopus 로고    scopus 로고
    • The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE
    • Neubauer C, et al. (2009) The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE. Cell 139(6):1084-1095.
    • (2009) Cell , vol.139 , Issue.6 , pp. 1084-1095
    • Neubauer, C.1
  • 22
    • 84890072129 scopus 로고    scopus 로고
    • YoeB-ribosome structure: A canonical RNase that requires the ribosome for its specific activity
    • Feng S, et al. (2013) YoeB-ribosome structure: A canonical RNase that requires the ribosome for its specific activity. Nucleic Acids Res 41(20):9549-9556.
    • (2013) Nucleic Acids Res , vol.41 , Issue.20 , pp. 9549-9556
    • Feng, S.1
  • 23
    • 84942279978 scopus 로고    scopus 로고
    • Molecular basis of ri-bosome recognition and mRNA hydrolysis by the E. Coli YafQ toxin
    • Maehigashi T, Ruangprasert A, Miles SJ, Dunham CM (2015) Molecular basis of ri-bosome recognition and mRNA hydrolysis by the E. coli YafQ toxin. Nucleic Acids Res 43(16):8002-8012.
    • (2015) Nucleic Acids Res , vol.43 , Issue.16 , pp. 8002-8012
    • Maehigashi, T.1    Ruangprasert, A.2    Miles, S.J.3    Dunham, C.M.4
  • 24
    • 65449116514 scopus 로고    scopus 로고
    • The inhibitory mechanism of protein synthesis by YoeB, an Escherichia coli toxin
    • Zhang Y, Inouye M (2009) The inhibitory mechanism of protein synthesis by YoeB, an Escherichia coli toxin. J Biol Chem 284(11):6627-6638.
    • (2009) J Biol Chem , vol.284 , Issue.11 , pp. 6627-6638
    • Zhang, Y.1    Inouye, M.2
  • 25
    • 79955394875 scopus 로고    scopus 로고
    • Bacterial toxin RelE mediates frequent codon-independent mRNA cleavage from the 5′ end of coding regions in vivo
    • Hurley JM, Cruz JW, Ouyang M, Woychik NA (2011) Bacterial toxin RelE mediates frequent codon-independent mRNA cleavage from the 5′ end of coding regions in vivo. J Biol Chem 286(17):14770-14778.
    • (2011) J Biol Chem , vol.286 , Issue.17 , pp. 14770-14778
    • Hurley, J.M.1    Cruz, J.W.2    Ouyang, M.3    Woychik, N.A.4
  • 26
    • 69949087541 scopus 로고    scopus 로고
    • Staphylococcus aureus YoeB homologues inhibit translation initiation
    • Yoshizumi S, et al. (2009) Staphylococcus aureus YoeB homologues inhibit translation initiation. J Bacteriol 191(18):5868-5872.
    • (2009) J Bacteriol , vol.191 , Issue.18 , pp. 5868-5872
    • Yoshizumi, S.1
  • 27
    • 1642483754 scopus 로고    scopus 로고
    • Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: Involvement of the yefM-yoeB toxin-antitoxin system
    • Christensen SK, et al. (2004) Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: Involvement of the yefM-yoeB toxin-antitoxin system. Mol Microbiol 51(6):1705-1717.
    • (2004) Mol Microbiol , vol.51 , Issue.6 , pp. 1705-1717
    • Christensen, S.K.1
  • 28
    • 56649103929 scopus 로고    scopus 로고
    • Translation affects YoeB and MazF messenger RNA interferase activities by different mechanisms
    • Christensen-Dalsgaard M, Gerdes K (2008) Translation affects YoeB and MazF messenger RNA interferase activities by different mechanisms. Nucleic Acids Res 36(20): 6472-6481.
    • (2008) Nucleic Acids Res , vol.36 , Issue.20 , pp. 6472-6481
    • Christensen-Dalsgaard, M.1    Gerdes, K.2
  • 29
    • 60649093164 scopus 로고    scopus 로고
    • Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage
    • Prysak MH, et al. (2009) Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage. Mol Microbiol 71(5):1071-1087.
    • (2009) Mol Microbiol , vol.71 , Issue.5 , pp. 1071-1087
    • Prysak, M.H.1
  • 30
    • 67650517830 scopus 로고    scopus 로고
    • Bacterial toxin HigB associates with ribosomes and mediates translation-dependent mRNA cleavage at A-rich sites
    • Hurley JM, Woychik NA (2009) Bacterial toxin HigB associates with ribosomes and mediates translation-dependent mRNA cleavage at A-rich sites. J Biol Chem 284(28): 18605-18613.
    • (2009) J Biol Chem , vol.284 , Issue.28 , pp. 18605-18613
    • Hurley, J.M.1    Woychik, N.A.2
  • 31
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
    • Takagi H, et al. (2005) Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects. Nat Struct Mol Biol 12(4): 327-331.
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.4 , pp. 327-331
    • Takagi, H.1
  • 32
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ri-bonuclease YoeB toxin by YefM antitoxin
    • Kamada K, Hanaoka F (2005) Conformational change in the catalytic site of the ri-bonuclease YoeB toxin by YefM antitoxin. Mol Cell 19(4):497-509.
    • (2005) Mol Cell , vol.19 , Issue.4 , pp. 497-509
    • Kamada, K.1    Hanaoka, F.2
  • 33
    • 84891938260 scopus 로고    scopus 로고
    • Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex
    • Schureck MA, et al. (2014) Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex. J Biol Chem 289(2):1060-1070.
    • (2014) J Biol Chem , vol.289 , Issue.2 , pp. 1060-1070
    • Schureck, M.A.1
  • 34
    • 84905387098 scopus 로고    scopus 로고
    • Mechanisms of toxin inhibition and transcriptional repression by Escherichia coli DinJ-YafQ
    • Ruangprasert A, et al. (2014) Mechanisms of toxin inhibition and transcriptional repression by Escherichia coli DinJ-YafQ. J Biol Chem 289(30):20559-20569.
    • (2014) J Biol Chem , vol.289 , Issue.30 , pp. 20559-20569
    • Ruangprasert, A.1
  • 35
    • 50449110851 scopus 로고    scopus 로고
    • Exposing plasmids as the Achilles' heel of drug-resistant bacteria
    • Williams JJ, Hergenrother PJ (2008) Exposing plasmids as the Achilles' heel of drug-resistant bacteria. Curr Opin Chem Biol 12(4):389-399.
    • (2008) Curr Opin Chem Biol , vol.12 , Issue.4 , pp. 389-399
    • Williams, J.J.1    Hergenrother, P.J.2
  • 37
    • 67649794729 scopus 로고    scopus 로고
    • Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA in-terferase active site
    • Li GY, Zhang Y, Inouye M, Ikura M (2009) Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA in-terferase active site. J Biol Chem 284(21):14628-14636.
    • (2009) J Biol Chem , vol.284 , Issue.21 , pp. 14628-14636
    • Li, G.Y.1    Zhang, Y.2    Inouye, M.3    Ikura, M.4
  • 38
    • 84867404222 scopus 로고    scopus 로고
    • The crystal structure of the intact E. Coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity
    • Bøggild A, et al. (2012) The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity. Structure 20(10): 1641-1648.
    • (2012) Structure , vol.20 , Issue.10 , pp. 1641-1648
    • Bøggild, A.1
  • 39
    • 0035805229 scopus 로고    scopus 로고
    • Recognition of cognate transfer RNA by the 30S ribosomal subunit
    • Ogle JM, et al. (2001) Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292(5518):897-902.
    • (2001) Science , vol.292 , Issue.5518 , pp. 897-902
    • Ogle, J.M.1
  • 40
    • 77956340277 scopus 로고    scopus 로고
    • Structural rearrangements of the ribosome at the tRNA proofreading step
    • Jenner L, Demeshkina N, Yusupova G, Yusupov M (2010) Structural rearrangements of the ribosome at the tRNA proofreading step. Nat Struct Mol Biol 17(9):1072-1078.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.9 , pp. 1072-1078
    • Jenner, L.1    Demeshkina, N.2    Yusupova, G.3    Yusupov, M.4
  • 41
    • 55849143658 scopus 로고    scopus 로고
    • Insights into translational termination from the structure of RF2 bound to the ribosome
    • Weixlbaumer A, et al. (2008) Insights into translational termination from the structure of RF2 bound to the ribosome. Science 322(5903):953-956.
    • (2008) Science , vol.322 , Issue.5903 , pp. 953-956
    • Weixlbaumer, A.1
  • 42
    • 49649099901 scopus 로고    scopus 로고
    • Structural basis for translation termination on the 70S ri-bosome
    • Laurberg M, et al. (2008) Structural basis for translation termination on the 70S ri-bosome. Nature 454(7206):852-857.
    • (2008) Nature , vol.454 , Issue.7206 , pp. 852-857
    • Laurberg, M.1
  • 43
    • 0028154121 scopus 로고
    • Crystal structure of RNase T1 with 3′-guanylic acid and guanosine
    • Zegers I, Haikal AF, Palmer R, Wyns L (1994) Crystal structure of RNase T1 with 3′-guanylic acid and guanosine. J Biol Chem 269(1):127-133.
    • (1994) J Biol Chem , vol.269 , Issue.1 , pp. 127-133
    • Zegers, I.1    Haikal, A.F.2    Palmer, R.3    Wyns, L.4
  • 44
    • 77954445197 scopus 로고    scopus 로고
    • Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3′-monophosphate
    • Noguchi S (2010) Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3′-monophosphate. Acta Crystallogr D Biol Crystallogr 66(Pt 7):843-849.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 843-849
    • Noguchi, S.1
  • 45
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97(12):6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.12 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 46
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, et al. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 25(17):3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1
  • 49
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macro-molecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macro-molecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 50
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer M, et al. (2006) Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313(5795):1935-1942.
    • (2006) Science , vol.313 , Issue.5795 , pp. 1935-1942
    • Selmer, M.1
  • 51
    • 0025737972 scopus 로고
    • A functional pseudoknot in 16S ribosomal RNA
    • Powers T, Noller HF (1991) A functional pseudoknot in 16S ribosomal RNA. EMBO J 10(8):2203-2214.
    • (1991) EMBO J , vol.10 , Issue.8 , pp. 2203-2214
    • Powers, T.1    Noller, H.F.2


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