Biopolym. Cell. 1991; 7(1):101-107.
Gene-Engineering Biotechnology
Study of β-lactamase tem1 synthesis in various escherichia coli strains infected by the phage λ bla with amber-mutations in different regulatory genes
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
Abstract
The search of optimal conditions for phage-dependent supersynthesis of β-lactamase was undertaken. For this purpose the recombinant phage with alternatively orientated β-lactamase (bla) structure gene were obtained. It was stated, that phage λblaN–N-, λblaQ–R– derivates are obtained. The β-lactamase producing strain was selected. The maximal recovery of β-lactamase was obtained while Su0 E. coli W3101 strain was infected by λ-phage bla Q–R–.
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References
[1]
Glushakova LG, Chernykh SI, Stelmashenko LN, Kordium VA. beta-galactosidase supersynthesis indiced by some amber mutation of phage lambda plac3Cl857. Molekulyarnaya biologiya (Kiev). 1982;30:37-41.
[2]
Glushakova LG, Chernykh SI, Kordium VA. Functioning of N-derivatives of phage plac3Cl857 in E. coli Suo. Dokl Akad Nauk SSSR. 1982; 267(12):56-9.
[3]
Kordium VA, Glushakova LG, Chernykh SI. Use of N-derivatives of lambda plac 5 phage for the purpose of beta-galactosidase supersynthesis. Dokl Akad Nauk SSSR. 1980;255(3):760-3.
[4]
Davison J, Brammar WJ, Brunel F. Quantitative aspects of gene expression in a lambda-trp fusion operon. Mol Gen Genet. 1974;130(1):9-20.
[5]
Murray NE, Kelley WS. Characterization of lambdapolA transducing phages; effective expression of the E. coli polA gene. Mol Gen Genet. 1979;175(1):77-87.
[6]
Clewell DB, Helinski DR. Supercoiled circular DNA-protein complex in Escherichia coli: purification and induced conversion to an opern circular DNA form. Proc Natl Acad Sci U S A. 1969;62(4):1159-66.
[7]
Maniatis T, Fritsch EF, Sambrook J. Molecular cloning: a laboratory manual. New York: Cold Spring Harbor Lab, 1982; 545 p.
[8]
Dagert M, Ehrlich SD. Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene. 1979;6(1):23-8.
[9]
Miller JH. Experiments in molecular genetics. Cold Spring Harbor Laboratory, 1972, 466 p.
[10]
Chaikovskaia SM, Venkina TG. A modified iodometric method for the determination of penicillinase activity. Antibiotiki. 1962;7:453-6.
[11]
Gottesman ME, Adhya S, Das A. Transcription antitermination by bacteriophage lambda N gene product. J Mol Biol. 1980;140(1):57-75.
[12]
Honigman A. Cloning and characterization of a transcription termination signal in bacteriophage lambda unresponsive to the N gene product. Gene. 1981;13(3):299-309.
[13]
Dambly-ChaudiГЁre C, Gottesman M, Debouck C, Adhya S. Regulation of the pR operon of bacteriophage lambda. J Mol Appl Genet. 1983;2(1):45-56.
[14]
Drahos D, Szybalski W. Antitermination and termination functions of the cloned nutL, N, and tL1 modules of coliphage lambda. Gene. 1981;16(1-3):261-74.
[15]
Salstrom JS, Szybalski W. Coliphage lambdanutL-: a unique class of mutants defective in the site of gene N product utilization for antitermination of leftward transcription. J Mol Biol. 1978;124(1):195-221.
[16]
The Bacteriophage lambda. Ed. A. D. Hershey. N. Y. Cold Spring Harbor Lab, 1971. NLM ID: 0313535
[17]
Kleckner N, Signer ER. Genetic characterization of plasmid formation by N- mutants of bacteriophage lambda. Virology. 1977;79(1):160-73.
[18]
Herskowitz I, Signer ER. A site essential for expression of all late genes in bacteriophage lambda. J Mol Biol. 1970;47(3):545-56.
[19]
Grayhack EJ, Roberts JW. The phage lambda Q gene product: activity of a transcription antiterminator in vitro. Cell. 1982;30(2):637-48.
[20]
Dambly C, Delstanche M, Gathoye AM. qin101: Promoter mutation which allows the constitutive expression of the late genes. J Virol. 1979;30(1):14-20.
[21]
Bienkowska-Szewczyk K, Lipinska B, Taylor A. The R gene product of bacteriophage lambda is the murein transglycosylase. Mol Gen Genet. 1981;184(1):111-4.
[22]
Moir A, Brammar WJ. The use of specialised transducing phages in the amplification of enzyme production. Mol Gen Genet. 1976;149(1):87-99.