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Volumn 7, Issue 6, 2012, Pages

Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ANTITOXIN; BACTERIAL TOXIN; ENDOPEPTIDASE LA; HIGH PERSISTER A TOXIN; HIGH PERSISTER B ANTITOXIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 84862505694     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039185     Document Type: Article
Times cited : (79)

References (59)
  • 2
    • 50349141358 scopus 로고
    • Treatment of staphylococcal infections with penicillin
    • Bigger JW, (1944) Treatment of staphylococcal infections with penicillin. Lancet ii: 497-500.
    • (1944) Lancet , vol.ii , pp. 497-500
    • Bigger, J.W.1
  • 3
    • 33845607284 scopus 로고    scopus 로고
    • Persister cells, dormancy and infectious disease
    • Lewis K, (2007) Persister cells, dormancy and infectious disease. Nat Rev Microbiol 5: 48-56.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 48-56
    • Lewis, K.1
  • 6
    • 16244399491 scopus 로고    scopus 로고
    • Phenotypic tolerance: antibiotic enrichment of noninherited resistance in bacterial populations
    • Wiuff C, Zappala RM, Regoes RR, Garner KN, Baquero F, et al. (2005) Phenotypic tolerance: antibiotic enrichment of noninherited resistance in bacterial populations. Antimicrob Agents Chemother 49: 1483-1494.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1483-1494
    • Wiuff, C.1    Zappala, R.M.2    Regoes, R.R.3    Garner, K.N.4    Baquero, F.5
  • 7
    • 0034002551 scopus 로고    scopus 로고
    • A dose-response study of antibiotic resistance in Pseudomonas aeruginosa biofilms
    • Brooun A, Liu S, Lewis K, (2000) A dose-response study of antibiotic resistance in Pseudomonas aeruginosa biofilms. Antimicrob Agents Chemother 44: 640-646.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 640-646
    • Brooun, A.1    Liu, S.2    Lewis, K.3
  • 8
    • 0035173818 scopus 로고    scopus 로고
    • Biofilms and planktonic cells of Pseudomonas aeruginosa have similar resistance to killing by antimicrobials
    • Spoering AL, Lewis K, (2001) Biofilms and planktonic cells of Pseudomonas aeruginosa have similar resistance to killing by antimicrobials. J Bacteriol 183: 6746-6751.
    • (2001) J Bacteriol , vol.183 , pp. 6746-6751
    • Spoering, A.L.1    Lewis, K.2
  • 9
    • 73849102829 scopus 로고    scopus 로고
    • Patients with long-term oral carriage harbor high-persister mutants of Candida albicans
    • LaFleur MD, Qi Q, Lewis K, (2010) Patients with long-term oral carriage harbor high-persister mutants of Candida albicans. Antimicrob Agents Chemother 54: 39-44.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 39-44
    • LaFleur, M.D.1    Qi, Q.2    Lewis, K.3
  • 10
    • 0028270774 scopus 로고
    • Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis
    • Black DS, Irwin B, Moyed HS, (1994) Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis. J Bacteriol 176: 4081-4091.
    • (1994) J Bacteriol , vol.176 , pp. 4081-4091
    • Black, D.S.1    Irwin, B.2    Moyed, H.S.3
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0022591020 scopus 로고
    • Molecular cloning and expression of hipA, a gene of Escherichia coli K-12 that affects frequency of persistence after inhibition of murein synthesis
    • Moyed HS, Broderick SH, (1986) Molecular cloning and expression of hipA, a gene of Escherichia coli K-12 that affects frequency of persistence after inhibition of murein synthesis. J Bacteriol 166: 399-403.
    • (1986) J Bacteriol , vol.166 , pp. 399-403
    • Moyed, H.S.1    Broderick, S.H.2
  • 14
    • 0023804926 scopus 로고
    • Conditional impairment of cell division and altered lethality in hipA mutants of Escherichia coli K-12
    • Scherrer R, Moyed HS, (1988) Conditional impairment of cell division and altered lethality in hipA mutants of Escherichia coli K-12. J Bacteriol 170: 3321-3326.
    • (1988) J Bacteriol , vol.170 , pp. 3321-3326
    • Scherrer, R.1    Moyed, H.S.2
  • 15
    • 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, et al. (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
  • 16
    • 33845428404 scopus 로고    scopus 로고
    • Kinase activity of overexpressed HipA is required for growth arrest and multidrug tolerance in Escherichia coli
    • Correia FF, D'Onofrio A, Rejtar T, Li L, Karger BL, et al. (2006) Kinase activity of overexpressed HipA is required for growth arrest and multidrug tolerance in Escherichia coli. J Bacteriol 188: 8360-8367.
    • (2006) J Bacteriol , vol.188 , pp. 8360-8367
    • Correia, F.F.1    D'Onofrio, A.2    Rejtar, T.3    Li, L.4    Karger, B.L.5
  • 17
    • 48749089081 scopus 로고    scopus 로고
    • The role of global regulators and nucleotide metabolism in antibiotic tolerance in Escherichia coli
    • Hansen S, Lewis K, Vulić M, (2008) The role of global regulators and nucleotide metabolism in antibiotic tolerance in Escherichia coli. Antimicrob Agents Chemother.
    • (2008) Antimicrob Agents Chemother
    • Hansen, S.1    Lewis, K.2    Vulić, M.3
  • 18
    • 0344826574 scopus 로고    scopus 로고
    • Characterization of the hipA7 allele of Escherichia coli and evidence that high persistence is governed by (p)ppGpp synthesis
    • Korch SB, Henderson TA, Hill TM, (2003) Characterization of the hipA7 allele of Escherichia coli and evidence that high persistence is governed by (p)ppGpp synthesis. Mol Microbiol 50: 1199-1213.
    • (2003) Mol Microbiol , vol.50 , pp. 1199-1213
    • Korch, S.B.1    Henderson, T.A.2    Hill, T.M.3
  • 19
    • 33744729683 scopus 로고    scopus 로고
    • Ectopic overexpression of wild-type and mutant hipA genes in Escherichia coli: effects on macromolecular synthesis and persister formation
    • Korch SB, Hill TM, (2006) Ectopic overexpression of wild-type and mutant hipA genes in Escherichia coli: effects on macromolecular synthesis and persister formation. J Bacteriol 188: 3826-3836.
    • (2006) J Bacteriol , vol.188 , pp. 3826-3836
    • Korch, S.B.1    Hill, T.M.2
  • 20
    • 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, 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
  • 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
    • 77649174212 scopus 로고    scopus 로고
    • Ciprofloxacin causes persister formation by inducing the TisB toxin in Escherichia coli
    • Dorr T, Vulic M, Lewis K, (2010) Ciprofloxacin causes persister formation by inducing the TisB toxin in Escherichia coli. Plos Biol 8: e1000317.
    • (2010) Plos Biol , vol.8
    • Dorr, T.1    Vulic, M.2    Lewis, K.3
  • 25
    • 60849121408 scopus 로고    scopus 로고
    • HicA of Escherichia coli defines a novel family of translation-independent mRNA interferases in bacteria and archaea
    • Jorgensen MG, Pandey DP, Jaskolska M, Gerdes K, (2009) HicA of Escherichia coli defines a novel family of translation-independent mRNA interferases in bacteria and archaea. J Bacteriol 191: 1191-1199.
    • (2009) J Bacteriol , vol.191 , pp. 1191-1199
    • Jorgensen, M.G.1    Pandey, D.P.2    Jaskolska, M.3    Gerdes, K.4
  • 26
    • 65549122072 scopus 로고    scopus 로고
    • Ectopic production of VapCs from Enterobacteria inhibits translation and trans-activates YoeB mRNA interferase
    • Winther KS, Gerdes K, (2009) Ectopic production of VapCs from Enterobacteria inhibits translation and trans-activates YoeB mRNA interferase. Mol Microbiol 72: 918-930.
    • (2009) Mol Microbiol , vol.72 , pp. 918-930
    • Winther, K.S.1    Gerdes, K.2
  • 27
    • 23044469885 scopus 로고    scopus 로고
    • The PIN-domain toxin-antitoxin array in mycobacteria
    • Arcus VL, Rainey PB, Turner SJ, (2005) The PIN-domain toxin-antitoxin array in mycobacteria. Trends Microbiol 13: 360-365.
    • (2005) Trends Microbiol , vol.13 , pp. 360-365
    • Arcus, V.L.1    Rainey, P.B.2    Turner, S.J.3
  • 28
    • 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
  • 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, Mozdzierz CJ, Cook AM, Zhu L, Zhang Y, 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: 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
  • 30
    • 79956074557 scopus 로고    scopus 로고
    • Antitoxin MqsA helps mediate the bacterial general stress response
    • Wang X, Kim Y, Hong SH, Ma Q, Brown BL, et al. (2011) Antitoxin MqsA helps mediate the bacterial general stress response. Nat Chem Biol 7: 359-366.
    • (2011) Nat Chem Biol , vol.7 , pp. 359-366
    • Wang, X.1    Kim, Y.2    Hong, S.H.3    Ma, Q.4    Brown, B.L.5
  • 31
    • 35649008288 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the Escherichia coli RelBE toxin-antitoxin system: indication for a functional role of differential stability
    • Cherny I, Overgaard M, Borch J, Bram Y, Gerdes K, et al. (2007) Structural and thermodynamic characterization of the Escherichia coli RelBE toxin-antitoxin system: indication for a functional role of differential stability. Biochemistry 46: 12152-12163.
    • (2007) Biochemistry , vol.46 , pp. 12152-12163
    • Cherny, I.1    Overgaard, M.2    Borch, J.3    Bram, Y.4    Gerdes, K.5
  • 32
  • 33
    • 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
  • 34
    • 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, 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: 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
  • 35
    • 82555168246 scopus 로고    scopus 로고
    • Crystal structure of the VapBC toxin-antitoxin complex from Shigella flexneri reveals a hetero-octameric DNA-binding assembly
    • Dienemann C, Boggild A, Winther KS, Gerdes K, Brodersen DE, (2011) Crystal structure of the VapBC toxin-antitoxin complex from Shigella flexneri reveals a hetero-octameric DNA-binding assembly. J Mol Biol 414: 713-722.
    • (2011) J Mol Biol , vol.414 , pp. 713-722
    • Dienemann, C.1    Boggild, A.2    Winther, K.S.3    Gerdes, K.4    Brodersen, D.E.5
  • 36
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin
    • Kamada K, 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
  • 37
    • 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-helix-helix motifs
    • Mattison K, Wilbur JS, So M, Brennan RG, (2006) Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix 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
  • 38
    • 0035807805 scopus 로고    scopus 로고
    • RelE, a global inhibitor of translation, is activated during nutritional stress
    • Christensen SK, Mikkelsen M, Pedersen K, Gerdes K, (2001) RelE, a global inhibitor of translation, is activated during nutritional stress. Proc Natl Acad Sci U S A 98: 14328-14333.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14328-14333
    • Christensen, S.K.1    Mikkelsen, M.2    Pedersen, K.3    Gerdes, K.4
  • 39
    • 70350552019 scopus 로고    scopus 로고
    • RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB
    • Overgaard M, Borch J, Gerdes K, (2009) RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB. J Mol Biol 394: 183-196.
    • (2009) J Mol Biol , vol.394 , pp. 183-196
    • Overgaard, M.1    Borch, J.2    Gerdes, K.3
  • 40
    • 0019859345 scopus 로고
    • ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12
    • Charette MF, Henderson GW, Markovitz A, (1981) ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc Natl Acad Sci U S A 78: 4728-4732.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 4728-4732
    • Charette, M.F.1    Henderson, G.W.2    Markovitz, A.3
  • 43
    • 71749105531 scopus 로고    scopus 로고
    • Regulation and quality control by Lon-dependent proteolysis
    • Van Melderen L, Aertsen A, (2009) Regulation and quality control by Lon-dependent proteolysis. Res Microbiol 160: 645-651.
    • (2009) Res Microbiol , vol.160 , pp. 645-651
    • van Melderen, L.1    Aertsen, A.2
  • 44
    • 0035958678 scopus 로고    scopus 로고
    • Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli
    • Kuroda A, Nomura K, Ohtomo R, Kato J, Ikeda T, et al. (2001) Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293: 705-708.
    • (2001) Science , vol.293 , pp. 705-708
    • Kuroda, A.1    Nomura, K.2    Ohtomo, R.3    Kato, J.4    Ikeda, T.5
  • 45
    • 4544343195 scopus 로고    scopus 로고
    • Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli
    • Nomura K, Kato J, Takiguchi N, Ohtake H, Kuroda A, (2004) Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli. J Biol Chem 279: 34406-34410.
    • (2004) J Biol Chem , vol.279 , pp. 34406-34410
    • Nomura, K.1    Kato, J.2    Takiguchi, N.3    Ohtake, H.4    Kuroda, A.5
  • 46
    • 77955452979 scopus 로고    scopus 로고
    • Regulation of phenotypic variability by a threshold-based mechanism underlies bacterial persistence
    • Rotem E, Loinger A, Ronin I, Levin-Reisman I, Gabay C, et al. (2010) Regulation of phenotypic variability by a threshold-based mechanism underlies bacterial persistence. Proc Natl Acad Sci U S A 107: 12541-12546.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12541-12546
    • Rotem, E.1    Loinger, A.2    Ronin, I.3    Levin-Reisman, I.4    Gabay, C.5
  • 47
    • 79957445913 scopus 로고    scopus 로고
    • The Escherichia coli replication inhibitor CspD is subject to growth-regulated degradation by the Lon protease
    • Langklotz S, Narberhaus F, (2011) The Escherichia coli replication inhibitor CspD is subject to growth-regulated degradation by the Lon protease. Mol Microbiol 80: 1313-1325.
    • (2011) Mol Microbiol , vol.80 , pp. 1313-1325
    • Langklotz, S.1    Narberhaus, F.2
  • 48
    • 77953551929 scopus 로고    scopus 로고
    • Escherichia coli toxin/antitoxin pair MqsR/MqsA regulate toxin CspD
    • Kim Y, Wang X, Zhang XS, Grigoriu S, Page R, et al. (2010) Escherichia coli toxin/antitoxin pair MqsR/MqsA regulate toxin CspD. Environ Microbiol 12: 1105-1121.
    • (2010) Environ Microbiol , vol.12 , pp. 1105-1121
    • Kim, Y.1    Wang, X.2    Zhang, X.S.3    Grigoriu, S.4    Page, R.5
  • 50
    • 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 U S A 97: 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 51
    • 34247844506 scopus 로고    scopus 로고
    • Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR
    • Pruteanu M, Neher SB, Baker TA, (2007) Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR. J Bacteriol 189: 3017-3025.
    • (2007) J Bacteriol , vol.189 , pp. 3017-3025
    • Pruteanu, M.1    Neher, S.B.2    Baker, T.A.3
  • 52
    • 0029887308 scopus 로고    scopus 로고
    • Fluorescence polarization analysis of protein-DNA and protein-protein interactions
    • Lundblad JR, Laurance M, Goodman RH, (1996) Fluorescence polarization analysis of protein-DNA and protein-protein interactions. Mol Endocrinol 10: 607-612.
    • (1996) Mol Endocrinol , vol.10 , pp. 607-612
    • Lundblad, J.R.1    Laurance, M.2    Goodman, R.H.3
  • 54
    • 0035682064 scopus 로고    scopus 로고
    • Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria
    • Haldimann A, Wanner BL, (2001) Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria. J Bacteriol 183: 6384-6393.
    • (2001) J Bacteriol , vol.183 , pp. 6384-6393
    • Haldimann, A.1    Wanner, B.L.2
  • 55
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • 2006.0008
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
    • (2006) Mol Syst Biol , vol.2
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5
  • 56
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research
    • Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, et al. (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12: 291-299.
    • (2005) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5
  • 57
    • 0034459564 scopus 로고    scopus 로고
    • Effects of combination of different -10 hexamers and downstream sequences on stationary-phase-specific sigma factor sigma(S)-dependent transcription in Pseudomonas putida
    • Ojangu EL, Tover A, Teras R, Kivisaar M, (2000) Effects of combination of different-10 hexamers and downstream sequences on stationary-phase-specific sigma factor sigma(S)-dependent transcription in Pseudomonas putida. J Bacteriol 182: 6707-6713.
    • (2000) J Bacteriol , vol.182 , pp. 6707-6713
    • Ojangu, E.L.1    Tover, A.2    Teras, R.3    Kivisaar, M.4
  • 58
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J, (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4


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