메뉴 건너뛰기




Volumn 277, Issue 15, 2010, Pages 3097-3117

ParD toxin-antitoxin system of plasmid R1 - Basic contributions, biotechnological applications and relationships with closely-related toxin-antitoxin systems

Author keywords

bacterial RNases; gene regulation; Kid toxin and Kis antitoxin; parD operon; plasmid maintenance; plasmid R1; toxin antitoxin systems; translation inhibition

Indexed keywords

ANTITOXIN; BACTERIAL PROTEIN; KID TOXIN; KIS TOXIN; PROTEIN PARD; TOXIN; UNCLASSIFIED DRUG;

EID: 77954694584     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07722.x     Document Type: Review
Times cited : (32)

References (141)
  • 1
    • 29144461520 scopus 로고    scopus 로고
    • Plasmid R1 - Replication and its control
    • Nordstrom K (2006) Plasmid R1 - replication and its control. Plasmid 55, 1 26.
    • (2006) Plasmid , vol.55 , pp. 1-26
    • Nordstrom, K.1
  • 4
    • 0018965756 scopus 로고
    • Partitioning of plasmid R1 in Escherichia coli. I. Kinetics of loss of plasmid derivatives deleted of the par region
    • Nordstrom K, Molin S Aagaard-Hansen H (1980) Partitioning of plasmid R1 in Escherichia coli. I. Kinetics of loss of plasmid derivatives deleted of the par region. Plasmid 4, 215 227.
    • (1980) Plasmid , vol.4 , pp. 215-227
    • Nordstrom, K.1    Molin, S.2    Aagaard-Hansen, H.3
  • 5
    • 0345333119 scopus 로고
    • Unique type of plasmid maintenance function: Postsegregational killing of plasmid-free cells
    • Gerdes K, Rasmussen PB Molin S (1986) Unique type of plasmid maintenance function: postsegregational killing of plasmid-free cells. Proc Natl Acad Sci USA 83, 3116 3120.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3116-3120
    • Gerdes, K.1    Rasmussen, P.B.2    Molin, S.3
  • 6
    • 0032696759 scopus 로고    scopus 로고
    • Addiction modules and programmed cell death and antideath in bacterial cultures
    • Engelberg-Kulka H Glaser G (1999) Addiction modules and programmed cell death and antideath in bacterial cultures. Annu Rev Microbiol 53, 43 70.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 43-70
    • Engelberg-Kulka, H.1    Glaser, G.2
  • 7
    • 0030713350 scopus 로고    scopus 로고
    • Conditionally lethal genes associated with bacterial plasmids
    • Holcik M Iyer VN (1997) Conditionally lethal genes associated with bacterial plasmids. Microbiology 143 (Pt 11 3403 3416.
    • (1997) Microbiology , vol.143 , Issue.PART 11 , pp. 3403-3416
    • Holcik, M.1    Iyer, V.N.2
  • 8
    • 0141707105 scopus 로고    scopus 로고
    • Toxins-antitoxins: Plasmid maintenance, programmed cell death, and cell cycle arrest
    • Hayes F (2003) Toxins-antitoxins: plasmid maintenance, programmed cell death, and cell cycle arrest. Science 301, 1496 1499.
    • (2003) Science , vol.301 , pp. 1496-1499
    • Hayes, F.1
  • 9
    • 0028963606 scopus 로고
    • Programmed cell death in bacterial populations
    • Yarmolinsky MB (1995) Programmed cell death in bacterial populations. Science 267, 836 837.
    • (1995) Science , vol.267 , pp. 836-837
    • Yarmolinsky, M.B.1
  • 10
    • 0033740341 scopus 로고    scopus 로고
    • Postsegregational killing does not increase plasmid stability but acts to mediate the exclusion of competing plasmids
    • Cooper TF Heinemann JA (2000) Postsegregational killing does not increase plasmid stability but acts to mediate the exclusion of competing plasmids. Proc Natl Acad Sci USA 97, 12643 12648.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12643-12648
    • Cooper, T.F.1    Heinemann, J.A.2
  • 11
    • 70349985747 scopus 로고    scopus 로고
    • Horizontal gene transfer and the earliest stages of the evolution of life
    • Poole AM (2009) Horizontal gene transfer and the earliest stages of the evolution of life. Res Microbiol 160, 473 480.
    • (2009) Res Microbiol , vol.160 , pp. 473-480
    • Poole, A.M.1
  • 12
    • 0015334701 scopus 로고
    • Mutations in R factors of Escherichia coli causing an increased number of R-factor copies per chromosome
    • Nordström K, Ingram LC Lundback A (1972) Mutations in R factors of Escherichia coli causing an increased number of R-factor copies per chromosome. J Bacteriol 110, 562 569.
    • (1972) J Bacteriol , vol.110 , pp. 562-569
    • Nordström, K.1    Ingram, L.C.2    Lundback, A.3
  • 13
    • 0021150228 scopus 로고
    • Control of replication of bacterial plasmids: Genetics, molecular biology, and physiology of the plasmid R1 system
    • Nordstrom K, Molin S Light J (1984) Control of replication of bacterial plasmids: genetics, molecular biology, and physiology of the plasmid R1 system. Plasmid 12, 71 90.
    • (1984) Plasmid , vol.12 , pp. 71-90
    • Nordstrom, K.1    Molin, S.2    Light, J.3
  • 14
    • 0021992145 scopus 로고
    • Stable inheritance of plasmid R1 requires two different loci
    • Gerdes K, Larsen JE Molin S (1985) Stable inheritance of plasmid R1 requires two different loci. J Bacteriol 161, 292 298.
    • (1985) J Bacteriol , vol.161 , pp. 292-298
    • Gerdes, K.1    Larsen, J.E.2    Molin, S.3
  • 15
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Moller-Jensen J, Jensen RB, Lowe J Gerdes K (2002) Prokaryotic DNA segregation by an actin-like filament. EMBO J 21, 3119 3127.
    • (2002) EMBO J , vol.21 , pp. 3119-3127
    • Moller-Jensen, J.1    Jensen, R.B.2    Lowe, J.3    Gerdes, K.4
  • 18
    • 0023442938 scopus 로고
    • Identification of components of a new stability system of plasmid R1, parD, that is close to the origin of replication of this plasmid
    • Bravo A, de Torrontegui G Diaz R (1987) Identification of components of a new stability system of plasmid R1, parD, that is close to the origin of replication of this plasmid. Mol Gen Genet 210, 101 110.
    • (1987) Mol Gen Genet , vol.210 , pp. 101-110
    • Bravo, A.1    De Torrontegui, G.2    Diaz, R.3
  • 19
    • 0020804285 scopus 로고
    • Mini-F plasmid genes that couple host cell division to plasmid proliferation
    • Ogura T Hiraga S (1983) Mini-F plasmid genes that couple host cell division to plasmid proliferation. Proc Natl Acad Sci USA 80, 4784 4788.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4784-4788
    • Ogura, T.1    Hiraga, S.2
  • 20
    • 0023992192 scopus 로고
    • Two genes, pemK and pemI, responsible for stable maintenance of resistance plasmid R100
    • Tsuchimoto S, Ohtsubo H Ohtsubo E (1988) Two genes, pemK and pemI, responsible for stable maintenance of resistance plasmid R100. J Bacteriol 170, 1461 1466.
    • (1988) J Bacteriol , vol.170 , pp. 1461-1466
    • Tsuchimoto, S.1    Ohtsubo, H.2    Ohtsubo, E.3
  • 21
    • 17844370503 scopus 로고    scopus 로고
    • Prokaryotic toxin-antitoxin stress response loci
    • Gerdes K, Christensen SK Lobner-Olesen A (2005) Prokaryotic toxin-antitoxin stress response loci. Nat Rev 3, 371 382.
    • (2005) Nat Rev , vol.3 , pp. 371-382
    • Gerdes, K.1    Christensen, S.K.2    Lobner-Olesen, A.3
  • 22
    • 27944437497 scopus 로고    scopus 로고
    • Toxin-antitoxin modules as bacterial metabolic stress managers
    • Buts L, Lah J, Dao-Thi MH, Wyns L Loris R (2005) Toxin-antitoxin modules as bacterial metabolic stress managers. Trends Biochem Sci 30, 672 679.
    • (2005) Trends Biochem Sci , vol.30 , pp. 672-679
    • Buts, L.1    Lah, J.2    Dao-Thi, M.H.3    Wyns, L.4    Loris, R.5
  • 23
    • 33748309126 scopus 로고    scopus 로고
    • Shutdown decay of mRNA
    • Condon C (2006) Shutdown decay of mRNA. Mol Microbiol 61, 573 583.
    • (2006) Mol Microbiol , vol.61 , pp. 573-583
    • Condon, C.1
  • 24
    • 33750489399 scopus 로고    scopus 로고
    • Bacterial programmed cell death and multicellular behavior in bacteria
    • Engelberg-Kulka H, Amitai S, Kolodkin-Gal I Hazan R (2006) Bacterial programmed cell death and multicellular behavior in bacteria. PLoS Genet 2, e135.
    • (2006) PLoS Genet , vol.2 , pp. 135
    • Engelberg-Kulka, H.1    Amitai, S.2    Kolodkin-Gal, I.3    Hazan, R.4
  • 26
    • 63449102873 scopus 로고    scopus 로고
    • Bacterial toxin-antitoxin systems: More than selfish entities?
    • Van Melderen L Saavedra De Bast M (2009) Bacterial toxin-antitoxin systems: more than selfish entities? PLoS Genet 5, e1000437.
    • (2009) PLoS Genet , vol.5 , pp. 1000437
    • Van Melderen, L.1    Saavedra De Bast, M.2
  • 27
    • 68849123382 scopus 로고    scopus 로고
    • Toxin- antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes
    • Pandey D Gerdes K (2005) Toxin- antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res 55, 78 89.
    • (2005) Nucleic Acids Res , vol.55 , pp. 78-89
    • Pandey, D.1    Gerdes, K.2
  • 28
    • 67649933665 scopus 로고    scopus 로고
    • Comprehensive comparative-genomic analysis of Type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes
    • Makarova KS, Wolf YI Koonin EV (2009) Comprehensive comparative-genomic analysis of Type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes. Biol Direct 4, 19.
    • (2009) Biol Direct , vol.4 , pp. 19
    • Makarova, K.S.1    Wolf, Y.I.2    Koonin, E.V.3
  • 29
    • 0024199426 scopus 로고
    • Killing of Escherichia coli cells modulated by components of the stability system parD of plasmid R1
    • Bravo A, Ortega S, de Torrontegui G Diaz R (1988) Killing of Escherichia coli cells modulated by components of the stability system parD of plasmid R1. Mol Gen Genet 215, 146 151.
    • (1988) Mol Gen Genet , vol.215 , pp. 146-151
    • Bravo, A.1    Ortega, S.2    De Torrontegui, G.3    Diaz, R.4
  • 30
    • 0024615347 scopus 로고
    • Effect of the pem system on stable maintenance of plasmid R100 in various Escherichia coli hosts
    • Tsuchimoto S Ohtsubo E (1989) Effect of the pem system on stable maintenance of plasmid R100 in various Escherichia coli hosts. Mol Gen Genet 215, 463 468.
    • (1989) Mol Gen Genet , vol.215 , pp. 463-468
    • Tsuchimoto, S.1    Ohtsubo, E.2
  • 31
    • 0029090349 scopus 로고
    • Comparison of ccd of F, parDE of RP4, and parD of R1 using a novel conditional replication control system of plasmid R1
    • Jensen RB, Grohmann E, Schwab H, Diaz-Orejas R Gerdes K (1995) Comparison of ccd of F, parDE of RP4, and parD of R1 using a novel conditional replication control system of plasmid R1. Mol Microbiol 17, 211 220.
    • (1995) Mol Microbiol , vol.17 , pp. 211-220
    • Jensen, R.B.1    Grohmann, E.2    Schwab, H.3    Diaz-orejas, R.4    Gerdes, K.5
  • 32
    • 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, 735 745.
    • (1992) J Mol Biol , vol.226 , pp. 735-745
    • Bernard, P.1    Couturier, M.2
  • 33
    • 0024657850 scopus 로고
    • Isolation and characterization of a conditional replication mutant of the antibiotic resistance factor R1 affected in the gene of the replication protein repA
    • Ortega S, de Torrontegui G Diaz R (1989) Isolation and characterization of a conditional replication mutant of the antibiotic resistance factor R1 affected in the gene of the replication protein repA. Mol Gen Genet 217, 111 117.
    • (1989) Mol Gen Genet , vol.217 , pp. 111-117
    • Ortega, S.1    De Torrontegui, G.2    Diaz, R.3
  • 34
    • 0028984232 scopus 로고
    • A mutation that decreases the efficiency of plasmid R1 replication leads to the activation of parD, a killer stability system of the plasmid
    • Ruiz-Echevarria MJ, de-la-Torre MA Diaz-Orejas R (1995) A mutation that decreases the efficiency of plasmid R1 replication leads to the activation of parD, a killer stability system of the plasmid. FEMS Microbiol Lett 130, 129 135.
    • (1995) FEMS Microbiol Lett , vol.130 , pp. 129-135
    • Ruiz-Echevarria, M.J.1    De-La-Torre, M.A.2    Diaz-Orejas, R.3
  • 35
    • 27144544573 scopus 로고    scopus 로고
    • Kid cleaves specific mRNAs at UUACU sites to rescue the copy number of plasmid R1
    • Pimentel B, Madine MA de la Cueva-Mendez G (2005) Kid cleaves specific mRNAs at UUACU sites to rescue the copy number of plasmid R1. EMBO J 24, 3459 3469.
    • (2005) EMBO J , vol.24 , pp. 3459-3469
    • Pimentel, B.1    Madine, M.A.2    De La Cueva-Mendez, G.3
  • 36
    • 0019980137 scopus 로고
    • Analysis of plasmid genome evolution based on nucleotide-sequence comparison of two related plasmids of Escherichia coli
    • Ryder TB, Davidson DB, Rosen JI, Ohtsubo E Ohtsubo H (1982) Analysis of plasmid genome evolution based on nucleotide-sequence comparison of two related plasmids of Escherichia coli. Gene 17, 299 310.
    • (1982) Gene , vol.17 , pp. 299-310
    • Ryder, T.B.1    Davidson, D.B.2    Rosen, J.I.3    Ohtsubo, E.4    Ohtsubo, H.5
  • 37
    • 0027461096 scopus 로고
    • Autoregulation by cooperative binding of the PemI and PemK proteins to the promoter region of the pem operon
    • Tsuchimoto S Ohtsubo E (1993) Autoregulation by cooperative binding of the PemI and PemK proteins to the promoter region of the pem operon. Mol Gen Genet 237, 81 88.
    • (1993) Mol Gen Genet , vol.237 , pp. 81-88
    • Tsuchimoto, S.1    Ohtsubo, E.2
  • 38
    • 0026683731 scopus 로고
    • The stable maintenance system pem of plasmid R100: Degradation of PemI protein may allow PemK protein to inhibit cell growth
    • Tsuchimoto S, Nishimura Y Ohtsubo E (1992) The stable maintenance system pem of plasmid R100: degradation of PemI protein may allow PemK protein to inhibit cell growth. J Bacteriol 174, 4205 4211.
    • (1992) J Bacteriol , vol.174 , pp. 4205-4211
    • Tsuchimoto, S.1    Nishimura, Y.2    Ohtsubo, E.3
  • 39
    • 0027522090 scopus 로고
    • ChpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100
    • Masuda Y, Miyakawa K, Nishimura Y Ohtsubo E (1993) chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100. J Bacteriol 175, 6850 6856.
    • (1993) J Bacteriol , vol.175 , pp. 6850-6856
    • Masuda, Y.1    Miyakawa, K.2    Nishimura, Y.3    Ohtsubo, E.4
  • 40
    • 0030787581 scopus 로고    scopus 로고
    • Functional interactions between homologous conditional killer systems of plasmid and chromosomal origin
    • Santos-Sierra S, Giraldo R Diaz-Orejas R (1997) Functional interactions between homologous conditional killer systems of plasmid and chromosomal origin. FEMS Microbiol Lett 152, 51 56.
    • (1997) FEMS Microbiol Lett , vol.152 , pp. 51-56
    • Santos-Sierra, S.1    Giraldo, R.2    Diaz-Orejas, R.3
  • 41
    • 0031740522 scopus 로고    scopus 로고
    • Functional interactions between chpB and parD, two homologous conditional killer systems found in the Escherichia coli chromosome and in plasmid R1
    • Santos-Sierra S, Giraldo R Diaz-Orejas R (1998) Functional interactions between chpB and parD, two homologous conditional killer systems found in the Escherichia coli chromosome and in plasmid R1. FEMS Microbiol Lett 168, 51 58.
    • (1998) FEMS Microbiol Lett , vol.168 , pp. 51-58
    • Santos-Sierra, S.1    Giraldo, R.2    Diaz-Orejas, R.3
  • 42
    • 0033222858 scopus 로고    scopus 로고
    • Occurrence of mazEF-like antitoxin/toxin systems in bacteria
    • Mittenhuber G (1999) Occurrence of mazEF-like antitoxin/toxin systems in bacteria. J Mol Microbiol Biotechnol 1, 295 302.
    • (1999) J Mol Microbiol Biotechnol , vol.1 , pp. 295-302
    • Mittenhuber, G.1
  • 44
    • 0030008368 scopus 로고    scopus 로고
    • An Escherichia coli chromosomal 'addiction module' regulated by guanosine [corrected] 3′,5′-bispyrophosphate: A model for programmed bacterial cell death
    • Aizenman E, Engelberg-Kulka H Glaser G (1996) An Escherichia coli chromosomal 'addiction module' regulated by guanosine [corrected] 3′,5′-bispyrophosphate: a model for programmed bacterial cell death. Proc Natl Acad Sci USA 93, 6059 6063.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6059-6063
    • Aizenman, E.1    Engelberg-kulka, H.2    Glaser, G.3
  • 45
    • 33645057206 scopus 로고    scopus 로고
    • MazG - A regulator of programmed cell death in Escherichia coli
    • Gross M, Marianovsky I Glaser G (2006) MazG - a regulator of programmed cell death in Escherichia coli. Mol Microbiol 59, 590 601.
    • (2006) Mol Microbiol , vol.59 , pp. 590-601
    • Gross, M.1    Marianovsky, I.2    Glaser, G.3
  • 46
    • 35548944074 scopus 로고    scopus 로고
    • A linear pentapeptide is a quorum-sensing factor required for mazEF-mediated cell death in Escherichia coli
    • Kolodkin-Gal I, Hazan R, Gaathon A, Carmeli S Engelberg-Kulka H (2007) A linear pentapeptide is a quorum-sensing factor required for mazEF-mediated cell death in Escherichia coli. Science 318, 652 655.
    • (2007) Science , vol.318 , pp. 652-655
    • Kolodkin-Gal, I.1    Hazan, R.2    Gaathon, A.3    Carmeli, S.4    Engelberg-Kulka, H.5
  • 47
    • 42549122192 scopus 로고    scopus 로고
    • The extracellular death factor: Physiological and genetic factors influencing its production and response in Escherichia coli
    • Kolodkin-Gal I Engelberg-Kulka H (2008) The extracellular death factor: physiological and genetic factors influencing its production and response in Escherichia coli. J Bacteriol 190, 3169 3175.
    • (2008) J Bacteriol , vol.190 , pp. 3169-3175
    • Kolodkin-Gal, I.1    Engelberg-Kulka, H.2
  • 48
    • 37649005671 scopus 로고    scopus 로고
    • MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development
    • Nariya H Inouye M (2008) MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development. Cell 132, 55 66.
    • (2008) Cell , vol.132 , pp. 55-66
    • Nariya, H.1    Inouye, M.2
  • 49
    • 0033976914 scopus 로고    scopus 로고
    • Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress
    • Gerdes K (2000) Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress. J Bacteriol 182, 561 572.
    • (2000) J Bacteriol , vol.182 , pp. 561-572
    • Gerdes, K.1
  • 50
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • Christensen SK, Pedersen K, Hansen FG Gerdes K (2003) Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J Mol Biol 332, 809 819.
    • (2003) J Mol Biol , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 51
    • 33745878537 scopus 로고    scopus 로고
    • Role of DNA replication and repair in thymineless death in Escherichia coli
    • Morganroth PA Hanawalt PC (2006) Role of DNA replication and repair in thymineless death in Escherichia coli. J Bacteriol 188, 5286 5288.
    • (2006) J Bacteriol , vol.188 , pp. 5286-5288
    • Morganroth, P.A.1    Hanawalt, P.C.2
  • 52
    • 34548496904 scopus 로고    scopus 로고
    • What is the benefit to Escherichia coli of having multiple toxin-antitoxin systems in its genome?
    • Tsilibaris V, Maenhaut-Michel G, Mine N Van Melderen L (2007) What is the benefit to Escherichia coli of having multiple toxin-antitoxin systems in its genome? J Bacteriol 189, 6101 6108.
    • (2007) J Bacteriol , vol.189 , pp. 6101-6108
    • Tsilibaris, V.1    Maenhaut-Michel, G.2    Mine, N.3    Van Melderen, L.4
  • 53
    • 0038797797 scopus 로고    scopus 로고
    • RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA
    • Christensen SK Gerdes K (2003) RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA. Mol Microbiol 48, 1389 1400.
    • (2003) Mol Microbiol , vol.48 , pp. 1389-1400
    • Christensen, S.K.1    Gerdes, K.2
  • 54
    • 1542472730 scopus 로고    scopus 로고
    • New connections in the prokaryotic toxin-antitoxin network: Relationship with the eukaryotic nonsense-mediated RNA decay system
    • Anantharaman V Aravind L (2003) New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system. Genome Biol 4, R81.
    • (2003) Genome Biol , vol.4 , pp. 81
    • Anantharaman, V.1    Aravind, L.2
  • 55
    • 0034649546 scopus 로고    scopus 로고
    • PIN domains in nonsense-mediated mRNA decay and RNAi
    • Clissold PM Ponting CP (2000) PIN domains in nonsense-mediated mRNA decay and RNAi. Curr Biol 10, R888 R890.
    • (2000) Curr Biol , vol.10
    • Clissold, P.M.1    Ponting, C.P.2
  • 57
    • 0020590028 scopus 로고
    • HipA, a newly recognized gene of Escherichia coli K-12 that affects frequency of persistence after inhibition of murein synthesis
    • Moyed HS Bertrand KP (1983) hipA, a newly recognized gene of Escherichia coli K-12 that affects frequency of persistence after inhibition of murein synthesis. J Bacteriol 155, 768 775.
    • (1983) J Bacteriol , vol.155 , pp. 768-775
    • Moyed, H.S.1    Bertrand, K.P.2
  • 58
    • 46049106335 scopus 로고    scopus 로고
    • Chromosomal toxin-antitoxin systems may act as anti-addiction modules
    • Saavedra De Bast M, Mine N Van Melderen L (2008) Chromosomal toxin-antitoxin systems may act as anti-addiction modules. J Bacteriol 190, 4603 4609.
    • (2008) J Bacteriol , vol.190 , pp. 4603-4609
    • Saavedra De Bast, M.1    Mine, N.2    Van Melderen, L.3
  • 59
    • 0022390750 scopus 로고
    • Effects of the ccd function of the F plasmid on bacterial growth
    • Jaffe A, Ogura T Hiraga S (1985) Effects of the ccd function of the F plasmid on bacterial growth. J Bacteriol 163, 841 849.
    • (1985) J Bacteriol , vol.163 , pp. 841-849
    • Jaffe, A.1    Ogura, T.2    Hiraga, S.3
  • 60
    • 0026504334 scopus 로고
    • Control of segregation of chromosomal DNA by sex factor F in Escherichia coli. Mutants of DNA gyrase subunit A suppress letD (ccdB) product growth inhibition
    • Miki T, Park JA, Nagao K, Murayama N Horiuchi T (1992) Control of segregation of chromosomal DNA by sex factor F in Escherichia coli. Mutants of DNA gyrase subunit A suppress letD (ccdB) product growth inhibition. J Mol Biol 225, 39 52.
    • (1992) J Mol Biol , vol.225 , pp. 39-52
    • Miki, T.1    Park, J.A.2    Nagao, K.3    Murayama, N.4    Horiuchi, T.5
  • 61
    • 0031558807 scopus 로고    scopus 로고
    • The interaction of the F plasmid killer protein, CcdB, with DNA gyrase: Induction of DNA cleavage and blocking of transcription
    • Critchlow SE, O'Dea MH, Howells AJ, Couturier M, Gellert M Maxwell A (1997) The interaction of the F plasmid killer protein, CcdB, with DNA gyrase: induction of DNA cleavage and blocking of transcription. J Mol Biol 273, 826 839.
    • (1997) J Mol Biol , vol.273 , pp. 826-839
    • Critchlow, S.E.1    O'Dea, M.H.2    Howells, A.J.3    Couturier, M.4    Gellert, M.5    Maxwell, A.6
  • 63
    • 0028947721 scopus 로고
    • Kid, a small protein of the parD stability system of plasmid R1, is an inhibitor of DNA replication acting at the initiation of DNA synthesis
    • Ruiz-Echevarria MJ, Gimenez-Gallego G, Sabariegos-Jareno R Diaz-Orejas R (1995) Kid, a small protein of the parD stability system of plasmid R1, is an inhibitor of DNA replication acting at the initiation of DNA synthesis. J Mol Biol 247, 568 577.
    • (1995) J Mol Biol , vol.247 , pp. 568-577
    • Ruiz-Echevarria, M.J.1    Gimenez-Gallego, G.2    Sabariegos-Jareno, R.3    Diaz-Orejas, R.4
  • 64
    • 0026090655 scopus 로고
    • Structural and functional comparison between the stability systems parD of plasmid R1 and ccd of plasmid F
    • Ruiz-Echevarria MJ, de-Torrontegui G, Gimenez-Gallego G Diaz-Orejas R (1991) Structural and functional comparison between the stability systems parD of plasmid R1 and ccd of plasmid F. Mol Gen Genet 225, 355 362.
    • (1991) Mol Gen Genet , vol.225 , pp. 355-362
    • Ruiz-Echevarria, M.J.1    De-Torrontegui, G.2    Gimenez-Gallego, G.3    Diaz-Orejas, R.4
  • 68
    • 67749110273 scopus 로고    scopus 로고
    • Driving forces of gyrase recognition by the addiction toxin CcdB
    • Simic M, De Jonge N, Loris R, Vesnaver G Lah J (2009) Driving forces of gyrase recognition by the addiction toxin CcdB. J Biol Chem 284, 20002 20010.
    • (2009) J Biol Chem , vol.284 , pp. 20002-20010
    • Simic, M.1    De Jonge, N.2    Loris, R.3    Vesnaver, G.4    Lah, J.5
  • 69
    • 0028963129 scopus 로고
    • F plasmid CcdB killer protein: CcdB gene mutants coding for non-cytotoxic proteins which retain their regulatory functions
    • Bahassi EM, Salmon MA, Van Melderen L, Bernard P Couturier M (1995) F plasmid CcdB killer protein: ccdB gene mutants coding for non-cytotoxic proteins which retain their regulatory functions. Mol Microbiol 15, 1031 1037.
    • (1995) Mol Microbiol , vol.15 , pp. 1031-1037
    • Bahassi, E.M.1    Salmon, M.A.2    Van Melderen, L.3    Bernard, P.4    Couturier, M.5
  • 71
    • 33750206130 scopus 로고    scopus 로고
    • A strand-passage conformation of DNA gyrase is required to allow the bacterial toxin, CcdB, to access its binding site
    • Smith AB Maxwell A (2006) A strand-passage conformation of DNA gyrase is required to allow the bacterial toxin, CcdB, to access its binding site. Nucleic Acids Res 34, 4667 4676.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4667-4676
    • Smith, A.B.1    Maxwell, A.2
  • 72
    • 0037005943 scopus 로고    scopus 로고
    • Genetic identification of two functional regions in the antitoxin of the parD killer system of plasmid R1
    • Santos-Sierra S, Pardo-Abarrio C, Giraldo R Diaz-Orejas R (2002) Genetic identification of two functional regions in the antitoxin of the parD killer system of plasmid R1. FEMS Microbiol Lett 206, 115 119.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 115-119
    • Santos-Sierra, S.1    Pardo-Abarrio, C.2    Giraldo, R.3    Diaz-Orejas, R.4
  • 73
    • 0025761119 scopus 로고
    • The 41 carboxy-terminal residues of the miniF plasmid CcdA protein are sufficient to antagonize the killer activity of the CcdB protein
    • Bernard P Couturier M (1991) The 41 carboxy-terminal residues of the miniF plasmid CcdA protein are sufficient to antagonize the killer activity of the CcdB protein. Mol Gen Genet 226, 297 304.
    • (1991) Mol Gen Genet , vol.226 , pp. 297-304
    • Bernard, P.1    Couturier, M.2
  • 74
    • 0028132685 scopus 로고
    • The antidote and autoregulatory functions of the F plasmid CcdA protein: A genetic and biochemical survey
    • Salmon MA, Van Melderen L, Bernard P Couturier M (1994) The antidote and autoregulatory functions of the F plasmid CcdA protein: a genetic and biochemical survey. Mol Gen Genet 244, 530 538.
    • (1994) Mol Gen Genet , vol.244 , pp. 530-538
    • Salmon, M.A.1    Van Melderen, L.2    Bernard, P.3    Couturier, M.4
  • 76
    • 0028177303 scopus 로고
    • DNA recognition by beta-sheets in the Arc repressor-operator crystal structure
    • Raumann BE, Rould MA, Pabo CO Sauer RT (1994) DNA recognition by beta-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
  • 77
  • 78
    • 34547564386 scopus 로고    scopus 로고
    • The solution structure of ParD, the antidote of the ParDE toxin antitoxin module, provides the structural basis for DNA and toxin binding
    • Oberer M, Zangger K, Gruber K Keller W (2007) The solution structure of ParD, the antidote of the ParDE toxin antitoxin module, provides the structural basis for DNA and toxin binding. Protein Sci 16, 1676 1688.
    • (2007) Protein Sci , vol.16 , pp. 1676-1688
    • Oberer, M.1    Zangger, K.2    Gruber, K.3    Keller, W.4
  • 79
    • 77949367813 scopus 로고    scopus 로고
    • A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex
    • Dalton KM 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
  • 81
    • 0025336625 scopus 로고
    • Structure of Arc repressor in solution: Evidence for a family of beta-sheet DNA-binding proteins
    • Breg JN, van Opheusden JH, Burgering MJ, Boelens R Kaptein R (1990) Structure of Arc repressor in solution: evidence for a family of beta-sheet DNA-binding proteins. Nature 346, 586 589.
    • (1990) Nature , vol.346 , pp. 586-589
    • Breg, J.N.1    Van Opheusden, J.H.2    Burgering, M.J.3    Boelens, R.4    Kaptein, R.5
  • 83
    • 0026641755 scopus 로고
    • Crystal structure of the Met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands
    • Somers WS Phillips SE (1992) Crystal structure of the Met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands. Nature 359, 387 393.
    • (1992) Nature , vol.359 , pp. 387-393
    • Somers, W.S.1    Phillips, S.E.2
  • 84
    • 53149133857 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein
    • Kumar P, Issac B, Dodson EJ, Turkenburg JP Mande SC (2008) Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J Mol Biol 383, 482 493.
    • (2008) J Mol Biol , vol.383 , pp. 482-493
    • Kumar, P.1    Issac, B.2    Dodson, E.J.3    Turkenburg, J.P.4    Mande, S.C.5
  • 85
    • 1542379603 scopus 로고    scopus 로고
    • The YefM antitoxin defines a family of natively unfolded proteins: Implications as a novel antibacterial target
    • Cherny I Gazit E (2004) The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. J Biol Chem 279, 8252 8261.
    • (2004) J Biol Chem , vol.279 , pp. 8252-8261
    • Cherny, I.1    Gazit, E.2
  • 86
    • 0037738520 scopus 로고    scopus 로고
    • Crystal structure of the MazE/MazF complex: Molecular bases of antidote-toxin recognition
    • Kamada K, Hanaoka F Burley SK (2003) Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition. Mol Cell 11, 875 884.
    • (2003) Mol Cell , vol.11 , pp. 875-884
    • Kamada, K.1    Hanaoka, F.2    Burley, S.K.3
  • 87
    • 0028222452 scopus 로고
    • Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria
    • Van Melderen L, Bernard P Couturier M (1994) Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free 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
  • 88
    • 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 MH, Lecchi P, Gottesman S, Couturier M Maurizi MR (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
  • 90
    • 0025933063 scopus 로고
    • The kis and kid genes of the parD maintenance system of plasmid R1 form an operon that is autoregulated at the level of transcription by the co-ordinated action of the Kis and Kid proteins
    • Ruiz-Echevarria MJ, Berzal-Herranz A, Gerdes K Diaz-Orejas R (1991) The kis and kid genes of the parD maintenance system of plasmid R1 form an operon that is autoregulated at the level of transcription by the co-ordinated action of the Kis and Kid proteins. Mol Microbiol 5, 2685 2693.
    • (1991) Mol Microbiol , vol.5 , pp. 2685-2693
    • Ruiz-Echevarria, M.J.1    Berzal-Herranz, A.2    Gerdes, K.3    Diaz-Orejas, R.4
  • 91
    • 34247133389 scopus 로고    scopus 로고
    • Interactions of Kid-Kis toxin-antitoxin complexes with the parD operator-promoter region of plasmid R1 are piloted by the Kis antitoxin and tuned by the stoichiometry of Kid-Kis oligomers
    • Monti MC, Hernandez-Arriaga AM, Kamphuis MB, Lopez-Villarejo J, Heck AJ, Boelens R, Diaz-Orejas R van den Heuvel RH (2007) Interactions of Kid-Kis toxin-antitoxin complexes with the parD operator-promoter region of plasmid R1 are piloted by the Kis antitoxin and tuned by the stoichiometry of Kid-Kis oligomers. Nucleic Acids Res 35, 1737 1749.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1737-1749
    • Monti, M.C.1    Hernandez-Arriaga, A.M.2    Kamphuis, M.B.3    Lopez-Villarejo, J.4    Heck, A.J.5    Boelens, R.6    Diaz-Orejas, R.7    Van Den Heuvel, R.H.8
  • 92
    • 0037515721 scopus 로고    scopus 로고
    • Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability, and influence on interactions with DNA
    • Lah J, Marianovsky I, Glaser G, Engelberg-Kulka H, Kinne J, Wyns L Loris R (2003) Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability, and influence on interactions with DNA. J Biol Chem 278, 14101 14111.
    • (2003) J Biol Chem , vol.278 , pp. 14101-14111
    • Lah, J.1    Marianovsky, I.2    Glaser, G.3    Engelberg-Kulka, H.4    Kinne, J.5    Wyns, L.6    Loris, R.7
  • 93
    • 0035937194 scopus 로고    scopus 로고
    • The regulation of the Escherichia colimazEF promoter involves an unusual alternating palindrome
    • Marianovsky I, Aizenman E, Engelberg-Kulka H Glaser G (2001) The regulation of the Escherichia colimazEF promoter involves an unusual alternating palindrome. J Biol Chem 276, 5975 5984.
    • (2001) J Biol Chem , vol.276 , pp. 5975-5984
    • Marianovsky, I.1    Aizenman, E.2    Engelberg-kulka, H.3    Glaser, G.4
  • 94
    • 0028878999 scopus 로고
    • Translational coupling and limited degradation of a polycistronic messenger modulate differential gene expression in the parD stability system of plasmid R1
    • Ruiz-Echevarria MJ, de-la-Cueva G Diaz-Orejas R (1995) Translational coupling and limited degradation of a polycistronic messenger modulate differential gene expression in the parD stability system of plasmid R1. Mol Gen Genet 248, 599 609.
    • (1995) Mol Gen Genet , vol.248 , pp. 599-609
    • Ruiz-Echevarria, M.J.1    De-La-Cueva, G.2    Diaz-Orejas, R.3
  • 95
    • 33846680128 scopus 로고    scopus 로고
    • Toxin-antitoxin regulation: Bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression
    • Kedzierska B, Lian LY 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
  • 96
    • 47749089764 scopus 로고    scopus 로고
    • Messenger RNA interferase RelE controls relBE transcription by conditional cooperativity
    • Overgaard M, Borch J, Jorgensen MG 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    Jorgensen, M.G.3    Gerdes, K.4
  • 97
    • 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 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
  • 99
    • 0036667464 scopus 로고    scopus 로고
    • Differential effects of Kid toxin on two modes of replication of lambdoid plasmids suggest that this toxin acts before, but not after, the assembly of the replication complex
    • Potrykus K, Santos S, Lemonnier M, Diaz-Orejas R Wegrzyn G (2002) Differential effects of Kid toxin on two modes of replication of lambdoid plasmids suggest that this toxin acts before, but not after, the assembly of the replication complex. Microbiology 148, 2489 2495.
    • (2002) Microbiology , vol.148 , pp. 2489-2495
    • Potrykus, K.1    Santos, S.2    Lemonnier, M.3    Diaz-Orejas, R.4    Wegrzyn, G.5
  • 100
    • 77954705020 scopus 로고    scopus 로고
    • Inhibición de proliferación celular en eucariotas y activation de apoptosis en ceélulas humanas mediante el control transcripcional independiente de los genes procariotas kis y kid. Análisis del mecanismo de acción e implicaciones en terapia. PhD Thesis. Universidad Autónoma de Madrid
    • De la Cueva-Mendez G (2000) Inhibición de proliferación celular en eucariotas y activation de apoptosis en ceélulas humanas mediante el control transcripcional independiente de los genes procariotas kis y kid. Análisis del mecanismo de acción e implicaciones en terapia. PhD Thesis. Universidad Autónoma de Madrid
    • (2000)
    • De La Cueva-Mendez, G.1
  • 101
    • 0036067108 scopus 로고    scopus 로고
    • Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins
    • Pedersen K, Christensen SK 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
  • 102
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
    • Pedersen K, Zavialov AV, Pavlov MY, Elf J, Gerdes K Ehrenberg M (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112, 131 140.
    • (2003) Cell , vol.112 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Y.3    Elf, J.4    Gerdes, K.5    Ehrenberg, M.6
  • 103
    • 0242361562 scopus 로고    scopus 로고
    • Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for translational quality control
    • Hayes CS Sauer RT (2003) Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for translational quality control. Mol Cell 12, 903 911.
    • (2003) Mol Cell , vol.12 , pp. 903-911
    • Hayes, C.S.1    Sauer, R.T.2
  • 105
    • 70350146494 scopus 로고    scopus 로고
    • RNase II is important for A-site mRNA cleavage during ribosome pausing
    • Garza-Sanchez F, Shoji S, Fredrick K Hayes CS (2009) RNase II is important for A-site mRNA cleavage during ribosome pausing. Mol Microbiol 73, 882 897.
    • (2009) Mol Microbiol , vol.73 , pp. 882-897
    • Garza-Sanchez, F.1    Shoji, S.2    Fredrick, K.3    Hayes, C.S.4
  • 106
    • 0242361323 scopus 로고    scopus 로고
    • MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli
    • Zhang Y, Zhang J, Hoeflich KP, Ikura M, Qing G Inouye M (2003) MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol Cell 12, 913 923.
    • (2003) Mol Cell , vol.12 , pp. 913-923
    • Zhang, Y.1    Zhang, J.2    Hoeflich, K.P.3    Ikura, M.4    Qing, G.5    Inouye, M.6
  • 108
    • 2442690258 scopus 로고    scopus 로고
    • Interference of mRNA function by sequence-specific endoribonuclease PemK
    • Zhang J, Zhang Y, Zhu L, Suzuki M Inouye M (2004) Interference of mRNA function by sequence-specific endoribonuclease PemK. J Biol Chem 279, 20678 20684.
    • (2004) J Biol Chem , vol.279 , pp. 20678-20684
    • Zhang, J.1    Zhang, Y.2    Zhu, L.3    Suzuki, M.4    Inouye, M.5
  • 111
    • 22544451588 scopus 로고    scopus 로고
    • Characterization of ChpBK, an mRNA interferase from Escherichia coli
    • Zhang Y, Zhu L, Zhang J Inouye M (2005) Characterization of ChpBK, an mRNA interferase from Escherichia coli. J Biol Chem 280, 26080 26088.
    • (2005) J Biol Chem , vol.280 , pp. 26080-26088
    • Zhang, Y.1    Zhu, L.2    Zhang, J.3    Inouye, M.4
  • 112
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • Zavialov AV, Mora L, Buckingham RH Ehrenberg M (2002) Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol Cell 10, 789 798.
    • (2002) Mol Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 113
    • 58149107443 scopus 로고    scopus 로고
    • Novel Escherichia coli RF1 mutants with decreased translation termination activity and increased sensitivity to the cytotoxic effect of the bacterial toxins Kid and RelE
    • Diago-Navarro E, Mora L, Buckingham RH, Diaz-Orejas R Lemonnier M (2009) Novel Escherichia coli RF1 mutants with decreased translation termination activity and increased sensitivity to the cytotoxic effect of the bacterial toxins Kid and RelE. Mol Microbiol 71, 66 78.
    • (2009) Mol Microbiol , vol.71 , pp. 66-78
    • Diago-Navarro, E.1    Mora, L.2    Buckingham, R.H.3    Diaz-Orejas, R.4    Lemonnier, M.5
  • 115
    • 0018153867 scopus 로고
    • Structure and replication of the colicin E1 plasmid
    • Staudenbauer WL (1978) Structure and replication of the colicin E1 plasmid, Curr Top Microbiol Immunol, 83, 93 156 Taylor, K 1995 Protection of coliphage lambda O initiator protein from proteolysis in the assembly of the replication complex in vivo, Virology, 207, 179 184.
    • (1978) Curr Top Microbiol Immunol , vol.83 , pp. 93-156
    • Staudenbauer, W.L.1    Taylor, K.2
  • 116
    • 0034141871 scopus 로고    scopus 로고
    • DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates
    • Johnson SK, Bhattacharyya S Griep MA (2000) DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates. Biochemistry 39, 736 744.
    • (2000) Biochemistry , vol.39 , pp. 736-744
    • Johnson, S.K.1    Bhattacharyya, S.2    Griep, M.A.3
  • 118
    • 0034467840 scopus 로고    scopus 로고
    • Bacterial toxin-antitoxin gene system as containment control in yeast cells
    • Kristoffersen P, Jensen GB, Gerdes K Piskur J (2000) Bacterial toxin-antitoxin gene system as containment control in yeast cells. Appl Environ Microbiol 66, 5524 5526.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5524-5526
    • Kristoffersen, P.1    Jensen, G.B.2    Gerdes, K.3    Piskur, J.4
  • 119
    • 0037157170 scopus 로고    scopus 로고
    • Bacterial toxin RelE induces apoptosis in human cells
    • Yamamoto TA, Gerdes K Tunnacliffe A (2002) Bacterial toxin RelE induces apoptosis in human cells. FEBS Lett 519, 191 194.
    • (2002) FEBS Lett , vol.519 , pp. 191-194
    • Yamamoto, T.A.1    Gerdes, K.2    Tunnacliffe, A.3
  • 120
    • 15244338743 scopus 로고    scopus 로고
    • Development without germ cells: The role of the germ line in zebrafish sex differentiation
    • Slanchev K, Stebler J, de la Cueva-Mendez G Raz E (2005) Development without germ cells: the role of the germ line in zebrafish sex differentiation. Proc Natl Acad Sci USA 102, 4074 4079.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4074-4079
    • Slanchev, K.1    Stebler, J.2    De La Cueva-Mendez, G.3    Raz, E.4
  • 123
    • 0028006860 scopus 로고
    • Positive-selection vectors using the F plasmid ccdB killer gene
    • Bernard P, Gabant P, Bahassi EM Couturier M (1994) Positive-selection vectors using the F plasmid ccdB killer gene. Gene 148, 71 74.
    • (1994) Gene , vol.148 , pp. 71-74
    • Bernard, P.1    Gabant, P.2    Bahassi, E.M.3    Couturier, M.4
  • 125
    • 33846911496 scopus 로고    scopus 로고
    • Construction of a Vibrio splendidus mutant lacking the metalloprotease gene vsm by use of a novel counterselectable suicide vector
    • Le Roux F, Binesse J, Saulnier D Mazel D (2007) Construction of a Vibrio splendidus mutant lacking the metalloprotease gene vsm by use of a novel counterselectable suicide vector. Appl Environ Microbiol 73, 777 784.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 777-784
    • Le Roux, F.1    Binesse, J.2    Saulnier, D.3    Mazel, D.4
  • 126
    • 0034213273 scopus 로고    scopus 로고
    • A novel episomal shuttle vector for transformation of Cryptococcus neoformans with the ccdB gene as a positive selection marker in bacteria
    • Mondon P, Chang YC, Varma A Kwon-Chung KJ (2000) A novel episomal shuttle vector for transformation of Cryptococcus neoformans with the ccdB gene as a positive selection marker in bacteria. FEMS Microbiol Lett 187, 41 45.
    • (2000) FEMS Microbiol Lett , vol.187 , pp. 41-45
    • Mondon, P.1    Chang, Y.C.2    Varma, A.3    Kwon-Chung, K.J.4
  • 127
    • 18444380606 scopus 로고    scopus 로고
    • Separate-component-stabilization system for protein and DNA production without the use of antibiotics
    • Szpirer CY Milinkovitch MC (2005) Separate-component-stabilization system for protein and DNA production without the use of antibiotics. BioTechniques 38, 775 781.
    • (2005) BioTechniques , vol.38 , pp. 775-781
    • Szpirer, C.Y.1    Milinkovitch, M.C.2
  • 128
    • 54349109072 scopus 로고    scopus 로고
    • The art of selective killing: Plasmid toxin/antitoxin systems and their technological applications
    • Stieber D, Gabant P Szpirer C (2008) The art of selective killing: plasmid toxin/antitoxin systems and their technological applications. BioTechniques 45, 344 346.
    • (2008) BioTechniques , vol.45 , pp. 344-346
    • Stieber, D.1    Gabant, P.2    Szpirer, C.3
  • 129
    • 17044408749 scopus 로고    scopus 로고
    • Single protein production in living cells facilitated by an mRNA interferase
    • Suzuki M, Zhang J, Liu M, Woychik NA Inouye M (2005) Single protein production in living cells facilitated by an mRNA interferase. Mol Cell 18, 253 261.
    • (2005) Mol Cell , vol.18 , pp. 253-261
    • Suzuki, M.1    Zhang, J.2    Liu, M.3    Woychik, N.A.4    Inouye, M.5
  • 130
    • 33645072739 scopus 로고    scopus 로고
    • The chromosomal relBE2 toxin-antitoxin locus of Streptococcus pneumoniae: Characterization and use of a bioluminescence resonance energy transfer assay to detect toxin-antitoxin interaction
    • Nieto C, Pellicer T, Balsa D, Christensen SK, Gerdes K Espinosa M (2006) The chromosomal relBE2 toxin-antitoxin locus of Streptococcus pneumoniae: characterization and use of a bioluminescence resonance energy transfer assay to detect toxin-antitoxin interaction. Mol Microbiol 59, 1280 1296.
    • (2006) Mol Microbiol , vol.59 , pp. 1280-1296
    • Nieto, C.1    Pellicer, T.2    Balsa, D.3    Christensen, S.K.4    Gerdes, K.5    Espinosa, M.6
  • 131
    • 73049085016 scopus 로고    scopus 로고
    • A toxin-antitoxin module as a target for antimicrobial development
    • Lioy VS, Rey O, Balsa D, Pellicer T Alonso JC (2010) A toxin-antitoxin module as a target for antimicrobial development. Plasmid 63, 31 39.
    • (2010) Plasmid , vol.63 , pp. 31-39
    • Lioy, V.S.1    Rey, O.2    Balsa, D.3    Pellicer, T.4    Alonso, J.C.5
  • 132
    • 0037337680 scopus 로고    scopus 로고
    • The Escherichia colimazEF suicide module mediates thymineless death
    • Sat B, Reches M Engelberg-Kulka H (2003) The Escherichia colimazEF suicide module mediates thymineless death. J Bacteriol 185, 1803 1807.
    • (2003) J Bacteriol , vol.185 , pp. 1803-1807
    • Sat, B.1    Reches, M.2    Engelberg-Kulka, H.3
  • 135
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M Wuthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14, 51 55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 136
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia colirelBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen M Gerdes K (1998) The Escherichia colirelBE 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
  • 137
    • 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 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 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
  • 138
    • 0026676272 scopus 로고
    • Definition of a minimal plasmid stabilization system from the broad-host-range plasmid RK2
    • Roberts RC Helinski DR (1992) Definition of a minimal plasmid stabilization system from the broad-host-range plasmid RK2. J Bacteriol 174, 8119 8132.
    • (1992) J Bacteriol , vol.174 , pp. 8119-8132
    • Roberts, R.C.1    Helinski, D.R.2
  • 139
    • 0025940779 scopus 로고
    • Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis
    • Black DS, Kelly AJ, Mardis MJ Moyed HS (1991) Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J Bacteriol 173, 5732 5739.
    • (1991) J Bacteriol , vol.173 , pp. 5732-5739
    • Black, D.S.1    Kelly, A.J.2    Mardis, M.J.3    Moyed, H.S.4
  • 140
    • 58449087611 scopus 로고    scopus 로고
    • Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB
    • Schumacher MA, Piro KM, Xu W, Hansen S, Lewis K Brennan RG (2009) Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB. Science 323, 396 401.
    • (2009) Science , vol.323 , pp. 396-401
    • Schumacher, M.A.1    Piro, K.M.2    Xu, W.3    Hansen, S.4    Lewis, K.5    Brennan, R.G.6
  • 141
    • 0026544822 scopus 로고
    • Analysis of an Escherichia coli mutant strain resistant to the cell-killing function encoded by the gef gene family
    • Poulsen LK, Larsen NW, Molin S Andersson P (1992) Analysis of an Escherichia coli mutant strain resistant to the cell-killing function encoded by the gef gene family. Mol Microbiol 6, 895 905.
    • (1992) Mol Microbiol , vol.6 , pp. 895-905
    • Poulsen, L.K.1    Larsen, N.W.2    Molin, S.3    Andersson, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.