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Volumn 289, Issue 30, 2014, Pages 20559-20569

Mechanisms of toxin inhibition and transcriptional repression by Escherichia coli DinJ-YafQ

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; GENE EXPRESSION;

EID: 84905387098     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.573006     Document Type: Article
Times cited : (40)

References (68)
  • 1
    • 10044266575 scopus 로고    scopus 로고
    • Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli
    • Keren, I., Shah, D., Spoering, A., Kaldalu, N., and Lewis, K. (2004) Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli. J. Bacteriol. 186, 8172-8180
    • (2004) J. Bacteriol. , vol.186 , pp. 8172-8180
    • Keren, I.1    Shah, D.2    Spoering, A.3    Kaldalu, N.4    Lewis, K.5
  • 2
    • 15744396567 scopus 로고    scopus 로고
    • Lessons from DNA microarray analysis: The gene expression profile of biofilms
    • Lazazzera, B. A. (2005) Lessons from DNA microarray analysis: the gene expression profile of biofilms. Curr. Opin. Microbiol. 8, 222-227
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 222-227
    • Lazazzera, B.A.1
  • 3
    • 77955628762 scopus 로고    scopus 로고
    • Persister cells
    • Lewis, K. (2010) Persister cells. Annu. Rev. Microbiol. 64, 357-372
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 357-372
    • Lewis, K.1
  • 4
    • 74249084586 scopus 로고    scopus 로고
    • Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: Implications for pathogenesis, stress responses, and evolution
    • Ramage, H. R., Connolly, L. E., and Cox, J. S. (2009) Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLoS Genet. 5, e1000767
    • (2009) PLoS Genet. , vol.5
    • Ramage, H.R.1    Connolly, L.E.2    Cox, J.S.3
  • 5
    • 80054759036 scopus 로고    scopus 로고
    • Regulation of growth and death in Escherichia coli by toxin-antitoxin systems
    • Yamaguchi, Y., and Inouye, M. (2011) Regulation of growth and death in Escherichia coli by toxin-antitoxin systems. Nat. Rev. Microbiol. 9, 779-790
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 779-790
    • Yamaguchi, Y.1    Inouye, M.2
  • 8
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen, M., and Gerdes, K. (1998) The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol. Microbiol. 29, 1065-1076
    • (1998) Mol. Microbiol. , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 9
    • 84863243970 scopus 로고    scopus 로고
    • Antitoxin DinJ influences the general stress response through transcript stabilizer CspE
    • Hu, Y., Benedik, M. J., and Wood, T. K. (2012) Antitoxin DinJ influences the general stress response through transcript stabilizer CspE. Environ. Microbiol. 14, 669-679
    • (2012) Environ. Microbiol. , vol.14 , pp. 669-679
    • Hu, Y.1    Benedik, M.J.2    Wood, T.K.3
  • 10
    • 33846680128 scopus 로고    scopus 로고
    • Toxin-antitoxin regulation: Bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression
    • Kedzierska, B., Lian, L. Y., and Hayes, F. (2007) Toxin-antitoxin regulation: bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression. Nucleic Acids Res. 35, 325-339
    • (2007) Nucleic Acids Res. , vol.35 , pp. 325-339
    • Kedzierska, B.1    Lian, L.Y.2    Hayes, F.3
  • 12
    • 0028076771 scopus 로고
    • Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence
    • Markiewicz, P., Kleina, L. G., Cruz, C., Ehret, S., and Miller, J. H. (1994) Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence. J. Mol. Biol. 240, 421-433
    • (1994) J. Mol. Biol. , vol.240 , pp. 421-433
    • Markiewicz, P.1    Kleina, L.G.2    Cruz, C.3    Ehret, S.4    Miller, J.H.5
  • 14
    • 77949367813 scopus 로고    scopus 로고
    • A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex
    • Dalton, K. M., and Crosson, S. (2010) A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex. Biochemistry 49, 2205-2215
    • (2010) Biochemistry , vol.49 , pp. 2205-2215
    • Dalton, K.M.1    Crosson, S.2
  • 15
    • 0037338682 scopus 로고    scopus 로고
    • Axe-Txe, a broad-spectrum proteic toxinantitoxin system specified by a multidrug-resistant, clinical isolate of Enterococcus faecium
    • Grady, R., and Hayes, F. (2003) Axe-Txe, a broad-spectrum proteic toxinantitoxin system specified by a multidrug-resistant, clinical isolate of Enterococcus faecium. Mol. Microbiol. 47, 1419-1432
    • (2003) Mol. Microbiol. , vol.47 , pp. 1419-1432
    • Grady, R.1    Hayes, F.2
  • 16
    • 67649794729 scopus 로고    scopus 로고
    • Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site
    • Li, G. Y., Zhang, Y., Inouye, M., and Ikura, M. (2009) Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. J. Biol. Chem. 284, 14628-14636
    • (2009) J. Biol. Chem. , vol.284 , pp. 14628-14636
    • Li, G.Y.1    Zhang, Y.2    Inouye, M.3    Ikura, M.4
  • 17
    • 0028230286 scopus 로고
    • The parDE operon of the broad-host-range plasmid RK2 specifies growth inhibition associated with plasmid loss
    • Roberts, R. C., Ström, A. R., and Helinski, D. R. (1994) The parDE operon of the broad-host-range plasmid RK2 specifies growth inhibition associated with plasmid loss. J. Mol. Biol. 237, 35-51
    • (1994) J. Mol. Biol. , vol.237 , pp. 35-51
    • Roberts, R.C.1    Ström, A.R.2    Helinski, D.R.3
  • 18
    • 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, S. K., Maenhaut-Michel, G., Mine, N., Gottesman, S., Gerdes, K., and Van Melderen, L. (2004) Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. Mol. Microbiol. 51, 1705-1717
    • (2004) Mol. Microbiol. , vol.51 , pp. 1705-1717
    • Christensen, S.K.1    Maenhaut-Michel, G.2    Mine, N.3    Gottesman, S.4    Gerdes, K.5    Van Melderen, L.6
  • 19
    • 84879148198 scopus 로고    scopus 로고
    • Cleavage of the antitoxin of the parD toxinantitoxin system is determined by the ClpAP protease and is modulated by the relative ratio of the toxin and the antitoxin
    • Diago-Navarro, E., Hernández-Arriaga, A. M., Kubik, S., Konieczny, I., and Díaz-Orejas, R. (2013) Cleavage of the antitoxin of the parD toxinantitoxin system is determined by the ClpAP protease and is modulated by the relative ratio of the toxin and the antitoxin. Plasmid 70, 78-85
    • (2013) Plasmid , vol.70 , pp. 78-85
    • Diago-Navarro, E.1    Hernández-Arriaga, A.M.2    Kubik, S.3    Konieczny, I.4    Díaz-Orejas, R.5
  • 20
    • 0028985596 scopus 로고
    • Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli
    • Lehnherr, H., and Yarmolinsky, M. B. (1995) Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 92, 3274-3277
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3274-3277
    • Lehnherr, H.1    Yarmolinsky, M.B.2
  • 21
    • 0028222452 scopus 로고
    • Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmidfree segregant bacteria
    • Van Melderen, L., Bernard, P., and Couturier, M. (1994) Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmidfree segregant bacteria. Mol. Microbiol. 11, 1151-1157
    • (1994) Mol. Microbiol. , vol.11 , pp. 1151-1157
    • Van Melderen, L.1    Bernard, P.2    Couturier, M.3
  • 24
    • 0036067108 scopus 로고    scopus 로고
    • Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins
    • Pedersen, K., Christensen, S. K., and Gerdes, K. (2002) Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol. Microbiol. 45, 501-510
    • (2002) Mol. Microbiol. , vol.45 , pp. 501-510
    • Pedersen, K.1    Christensen, S.K.2    Gerdes, K.3
  • 25
    • 47749089764 scopus 로고    scopus 로고
    • Messenger RNA interferase RelE controls relBE transcription by conditional cooperativity
    • Overgaard, M., Borch, J., Jørgensen, M. G., and Gerdes, K. (2008) Messenger RNA interferase RelE controls relBE transcription by conditional cooperativity. Mol. Microbiol. 69, 841-857
    • (2008) Mol. Microbiol. , vol.69 , pp. 841-857
    • Overgaard, M.1    Borch, J.2    Jørgensen, M.G.3    Gerdes, K.4
  • 27
    • 0031785682 scopus 로고    scopus 로고
    • Corepression of the P1 addiction operon by Phd and Doc
    • Magnuson, R., and Yarmolinsky, M. B. (1998) Corepression of the P1 addiction operon by Phd and Doc. J. Bacteriol. 180, 6342-6351
    • (1998) J. Bacteriol. , vol.180 , pp. 6342-6351
    • Magnuson, R.1    Yarmolinsky, M.B.2
  • 28
    • 0029862847 scopus 로고    scopus 로고
    • Plasmid RK2 toxin protein ParE: Purification and interaction with the ParD antitoxin protein
    • Johnson, E. P., Strom, A. R., and Helinski, D. R. (1996) Plasmid RK2 toxin protein ParE: purification and interaction with the ParD antitoxin protein. J. Bacteriol. 178, 1420-1429
    • (1996) J. Bacteriol. , vol.178 , pp. 1420-1429
    • Johnson, E.P.1    Strom, A.R.2    Helinski, D.R.3
  • 29
    • 0034939217 scopus 로고    scopus 로고
    • The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system
    • Afif, H., Allali, N., Couturier, M., and Van Melderen, L. (2001) The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system. Mol. Microbiol. 41, 73-82
    • (2001) Mol. Microbiol. , vol.41 , pp. 73-82
    • Afif, H.1    Allali, N.2    Couturier, M.3    Van Melderen, L.4
  • 30
    • 84857963742 scopus 로고    scopus 로고
    • Characterization of Escherichia coli dinJ-yafQ toxin-antitoxin system using insights from mutagenesis data
    • Armalyte, J., Jurenaite, M., Beinoraviciūte, G., Teiserskas, J., and Suziedeliene, E. (2012) Characterization of Escherichia coli dinJ-yafQ toxin-antitoxin system using insights from mutagenesis data. J. Bacteriol. 194, 1523-1532
    • (2012) J. Bacteriol. , vol.194 , pp. 1523-1532
    • Armalyte, J.1    Jurenaite, M.2    Beinoraviciute, G.3    Teiserskas, J.4    Suziedeliene, E.5
  • 31
    • 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, M. H., Mozdzierz, C. J., Cook, A. M., Zhu, L., Zhang, Y., Inouye, M., and Woychik, N. A. (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, 1071-1087
    • (2009) Mol. Microbiol. , vol.71 , pp. 1071-1087
    • Prysak, M.H.1    Mozdzierz, C.J.2    Cook, A.M.3    Zhu, L.4    Zhang, Y.5    Inouye, M.6    Woychik, N.A.7
  • 32
    • 84877081375 scopus 로고    scopus 로고
    • Structural overview of toxinantitoxin systems in infectious bacteria: A target for developing antimicrobial agents
    • Park, S. J., Son, W. S., and Lee, B. J. (2013) Structural overview of toxinantitoxin systems in infectious bacteria: a target for developing antimicrobial agents. Biochim. Biophys. Acta 1834, 1155-1167
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1155-1167
    • Park, S.J.1    Son, W.S.2    Lee, B.J.3
  • 33
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié, S. (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 34
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L., and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Carter, C. W., Jr., and Sweet, R. M., eds, Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) in Methods in Enzymology (Carter, C. W., Jr., and Sweet, R. M., eds) pp. 307-326, Academic Press, New York
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 37
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for phasing with the SHELX programs
    • Pape, T., and Schneider, T. R. (2004) HKL2MAP: a graphical user interface for phasing with the SHELX programs. J. Appl. Crystallogr. 37, 843-844
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 42
    • 0025370615 scopus 로고
    • Construction of broad-hostrange plasmid vectors for easy visible selection and analysis of promoters
    • Farinha, M. A., and Kropinski, A. M. (1990) Construction of broad-hostrange plasmid vectors for easy visible selection and analysis of promoters. J. Bacteriol 172, 3496-3499
    • (1990) J. Bacteriol , vol.172 , pp. 3496-3499
    • Farinha, M.A.1    Kropinski, A.M.2
  • 43
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. (1972) Experiments in Molecular Genetics, pp. 352-355, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 44
    • 33846011436 scopus 로고    scopus 로고
    • Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helixhelix motifs
    • Mattison, K., Wilbur, J. S., So, M., and Brennan, R. G. (2006) Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helixhelix motifs. J. Biol. Chem. 281, 37942-37951
    • (2006) J. Biol. Chem. , vol.281 , pp. 37942-37951
    • Mattison, K.1    Wilbur, J.S.2    So, M.3    Brennan, R.G.4
  • 46
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • Hasegawa, H., and Holm, L. (2009) Advances and pitfalls of protein structural alignment. Curr. Opin. Struct. Biol. 19, 341-348
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 47
    • 0028177303 scopus 로고
    • DNA recognition by β-sheets in the Arc repressor-operator crystal structure
    • Raumann, B. E., Rould, M. A., Pabo, C. O., and Sauer, R. T. (1994) DNA recognition by β-sheets in the Arc repressor-operator crystal structure. Nature 367, 754-757
    • (1994) Nature , vol.367 , pp. 754-757
    • Raumann, B.E.1    Rould, M.A.2    Pabo, C.O.3    Sauer, R.T.4
  • 48
    • 0028154121 scopus 로고
    • Crystal structure of RNase T1 with 3'-guanylic acid and guanosine
    • Zegers, I., Haikal, A. F., Palmer, R., and Wyns, L. (1994) Crystal structure of RNase T1 with 3'-guanylic acid and guanosine. J. Biol. Chem. 269, 127-133
    • (1994) J. Biol. Chem. , vol.269 , pp. 127-133
    • Zegers, I.1    Haikal, A.F.2    Palmer, R.3    Wyns, L.4
  • 49
    • 0000446384 scopus 로고
    • Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8Åresolution
    • Sevcik, J., Dodson, E. J., and Dodson, G. G. (1991) Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8Åresolution. Acta Crystallogr. Sect. B Struct. Sci. 47, 240-253
    • (1991) Acta Crystallogr. Sect. B Struct. Sci. , vol.47 , pp. 240-253
    • Sevcik, J.1    Dodson, E.J.2    Dodson, G.G.3
  • 50
    • 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., Sofos, N., Andersen, K. R., Feddersen, A., Easter, A. D., Passmore, L. A., and Brodersen, D. E. (2012) The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity. Structure 20, 1641-1648
    • (2012) Structure , vol.20 , pp. 1641-1648
    • Bøggild, A.1    Sofos, N.2    Andersen, K.R.3    Feddersen, A.4    Easter, A.D.5    Passmore, L.A.6    Brodersen, D.E.7
  • 51
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin
    • Kamada, K., and Hanaoka, F. (2005) Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol. Cell 19, 497-509
    • (2005) Mol. Cell , vol.19 , pp. 497-509
    • Kamada, K.1    Hanaoka, F.2
  • 52
    • 74549170423 scopus 로고    scopus 로고
    • Three-dimensional structure of the MqsR: MqsA complex: A novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties
    • Brown, B. L., Grigoriu, S., Kim, Y., Arruda, J. M., Davenport, A., Wood, T. K., Peti, W., and Page, R. (2009) Three-dimensional structure of the MqsR: MqsA complex: a novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties. PLoS Pathog. 5, e1000706
    • (2009) PLoS Pathog. , vol.5
    • Brown, B.L.1    Grigoriu, S.2    Kim, Y.3    Arruda, J.M.4    Davenport, A.5    Wood, T.K.6    Peti, W.7    Page, R.8
  • 54
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 55
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
    • Takagi, H., Kakuta, Y., Okada, T., Yao, M., Tanaka, I., and Kimura, M. (2005) Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects. Nat. Struct. Mol. Biol. 12, 327-331
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 327-331
    • Takagi, H.1    Kakuta, Y.2    Okada, T.3    Yao, M.4    Tanaka, I.5    Kimura, M.6
  • 57
    • 34548046005 scopus 로고    scopus 로고
    • Ribbon-helix-helix transcription factors: Variations on a theme
    • Schreiter, E. R., and Drennan, C. L. (2007) Ribbon-helix-helix transcription factors: variations on a theme. Nat. Rev. Microbiol. 5, 710-720
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 710-720
    • Schreiter, E.R.1    Drennan, C.L.2
  • 58
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger, C. D., Schildbach, J. F., and Sauer, R. T. (1995) Are buried salt bridges important for protein stability and conformational specificity? Nat. Struct. Biol. 2, 122-128
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 59
    • 84889257673 scopus 로고    scopus 로고
    • Bacterial toxin RelE: A highly efficient ribonuclease with exquisite substrate specificity using atypical catalytic residues
    • Griffin, M. A., Davis, J. H., and Strobel, S. A. (2013) Bacterial toxin RelE: a highly efficient ribonuclease with exquisite substrate specificity using atypical catalytic residues. Biochemistry 52, 8633-8642
    • (2013) Biochemistry , vol.52 , pp. 8633-8642
    • Griffin, M.A.1    Davis, J.H.2    Strobel, S.A.3
  • 61
    • 0029680387 scopus 로고    scopus 로고
    • SOS response as an adaptive response toDNAdamage in prokaryotes
    • Shinagawa, H. (1996) SOS response as an adaptive response toDNAdamage in prokaryotes. EXS 77, 221-235
    • (1996) EXS , vol.77 , pp. 221-235
    • Shinagawa, H.1
  • 62
    • 84883342218 scopus 로고    scopus 로고
    • (p) ppGpp controls bacterial persistence by stochastic induction of toxin-antitoxin activity
    • Maisonneuve, E., Castro-Camargo, M., and Gerdes, K. (2013) (p) ppGpp controls bacterial persistence by stochastic induction of toxin-antitoxin activity. Cell 154, 1140-1150
    • (2013) Cell , vol.154 , pp. 1140-1150
    • Maisonneuve, E.1    Castro-Camargo, M.2    Gerdes, K.3
  • 63
    • 84861550633 scopus 로고    scopus 로고
    • Regulation of enteric vapBC transcription: Induction by VapC toxin dimer-breaking
    • Winther, K. S., and Gerdes, K. (2012) Regulation of enteric vapBC transcription: induction by VapC toxin dimer-breaking. Nucleic Acids Res. 40, 4347-4357
    • (2012) Nucleic Acids Res. , vol.40 , pp. 4347-4357
    • Winther, K.S.1    Gerdes, K.2
  • 64
    • 0029861722 scopus 로고    scopus 로고
    • ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions
    • Van Melderen, L., Thi, M. H., Lecchi, P., Gottesman, S., Couturier, M., and Maurizi, M. R. (1996) ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. J. Biol. Chem. 271, 27730-27738
    • (1996) J. Biol. Chem. , vol.271 , pp. 27730-27738
    • Van Melderen, L.1    Thi, M.H.2    Lecchi, P.3    Gottesman, S.4    Couturier, M.5    Maurizi, M.R.6
  • 66
    • 38649092391 scopus 로고    scopus 로고
    • Transcription profiling of the stringent response in Escherichia coli
    • Durfee, T., Hansen, A. M., Zhi, H., Blattner, F. R., and Jin, D. J. (2008) Transcription profiling of the stringent response in Escherichia coli. J. Bacteriol. 190, 1084-1096
    • (2008) J. Bacteriol. , vol.190 , pp. 1084-1096
    • Durfee, T.1    Hansen, A.M.2    Zhi, H.3    Blattner, F.R.4    Jin, D.J.5
  • 67
    • 4043069926 scopus 로고    scopus 로고
    • DksA: A critical component of the transcription initiation machinery that potentiates the regulation of rRNA promoters by (p) ppGpp and the initiating NTP
    • Paul, B. J., Barker, M. M., Ross, W., Schneider, D. A., Webb, C., Foster, J. W., and Gourse, R. L. (2004) DksA: a critical component of the transcription initiation machinery that potentiates the regulation of rRNA promoters by (p) ppGpp and the initiating NTP. Cell 118, 311-322
    • (2004) Cell , vol.118 , pp. 311-322
    • Paul, B.J.1    Barker, M.M.2    Ross, W.3    Schneider, D.A.4    Webb, C.5    Foster, J.W.6    Gourse, R.L.7
  • 68
    • 77954257799 scopus 로고    scopus 로고
    • Con-Surf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) Con-Surf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5


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