Mutants of Escherichia coli

Touati D, M Jacques, B Tardat, L Bouchard, S Despied (1995) Lethal oxidative damage and mutagenesis are generated by iron Afur mutants of Escherichia coli protective role of superoxide dismutase. J Bacterial 111 2305-2314. 

G21. Grossowicz, N., Aronovitch, J., and Rachmilewitz, M., Determination of vitamin B12 in human serum by a mutant of Escherichia coli. Proc. Soc. Exptl. Biol. Med. 87, 513-518 (1954). 

Kato, T. and Shinoura, Y. (1977). Isolation and characterization of mutants of Escherichia coli deficient in induction of mutation by ultraviolet light. Mol. Gen. Genet. 156 121-132. 

Nagel R, Adler HI, Rao TK. 1982. Induction of filamentation by mutagens and carcinogens in a lon-mutant of Escherichia coli. Mutat Res 105 309-312. 

Waugh, R. and Boxer, D. H. (1986) Pleiotropic hydrogenase mutants of Escherichia coli K12 Growth in the presence of nickel can restore hydrogenase activity. Biochimie, 68, 157-66. 

Hamelin, C., and Y. S. Chung. Characterization of mucoid mutants of Escherichia coli K-12 isolated after exposure to ozone. J. Bacteriol. 122 19-24, 1975. 

Maezawa, H. Furusawa, Y. Kobayashi, K. Hieda, K. Suzuki, M. Usami, N. Yokoya, A. Mori, T. Lethal effect of K-shell absorption of intracellular phosphorus on wild- type and radiation sensitive mutants of Escherichia coli [published erratum appears in Acta Oncol. 1997 36(2) 238] Acta Oncol. 1996, 35 (7), 889-894. 

Yokota, A., Terasawa, Y., Takaoka, N., Shimizu, H. and Tomita, F. (1994) Pyruvic acid production by an Fj-ATPase-defective mutant of Escherichia coli W14851ip2. Biosci Biotechnol Biochem. 58, 2164-2167. 

Arnau J, Jorgensen F, Madsen SM, Vrang A, Israelsen H (1998) Cloning of the Lactococcus lactis adhE gene, encoding a multifunctional alcohol dehydrogenase, by complementation of a fermentative mutant of Escherichia coli. J Bacteriol 180 3049-3055... 

Fundamental membrane research has benefited greatly from the study of monolayers. One of the most important discoveries from this sort of research is the very existence of two-dimensional phases and phase transitions. Generally, studies of the sort that can be carried out with monolayers and bilayers cannot be directly extended to living cells, but some exceptional cases have shown that the extrapolation is valid. For example, it is known from monolayer studies that the presence of unsaturated hydrocarbon chains in lipid monolayers prevents some phase transitions from occurring as the temperature is lowered. Certain mutants of Escherichia coli are unable to synthesize fatty acids and hence can be manipulated through the compounds they are provided as nutrients. Abnormal levels of saturated hydrocarbon can... 

Clarke, A.J. Margulies, A.D. (1965). Isolation and characterisation of recombination-deficient mutants of Escherichia coli K12. Proc. Natl. Acad. Sci. USA 53,451-459. 

Hill, R.F. (1958). A radiation-sensitive mutant of Escherichia coli. Biochem. Biophys. Acta 30,636-637. 

Kanamori, T., et al. 1988. Expression and excretion of human pancreatic secretory trypsin inhibitor in lipoprotein-deletion mutant of Escherichia coli. Gene 66 295. 

Zhang, Y., Oldenburg, M., and Fillingame, R. H. (1994). Suppressor mutations in Fj subunit t recouple ATP-driven H+ translocation in uncoupled Q42E subunit c mutant of Escherichia coli FiFo ATP synthase./. Biol. Chem. 269, 10221-10224. 

S. M. Strain, S. W. Fesik, and I. M. Armitage, Characterization of lipopolysaccharide from a Heptoseless mutant of Escherichia coli by carbon 13 nuclear magnetic resonance, J. Biol. Chem., 258 (1983) 2906-2910. 

EJJ Lugtenberg, L de Haas-Menger, WHM Ruyters. Murein synthesis and identification of cell wall precursors of temperature-sensitive lysis mutants of Escherichia coli. J Bacteriol 109 326-335, 1972. 

EJJ Lugtenberg, A van Schijndel-vanDam. Temperature-sensitive mutants of Escherichia coli K-12 with low activities of the L-alanine adding enzyme and the D-alanyl-D-alanine adding enzyme. J Bacteriol 110 35 40, 1972. 

EJJ Lugtenberg, A van Schijndel-van Dam. Temperature-sensitive mutant of Escherichia coli K-12 with an impaired D-alanine D-alanine ligase. J Bacteriol 113 96— 104, 1973. 

Beja O, Bibi E. Functional expression of mouse Mdrl in an outer membrane permeability mutant of Escherichia coli. Proc Natl Acad Sci USA 1996 93 (12) 5969-5974. 

Breazeale, S.D., Ribeiro, A.A., Raetz, C.R.H. Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose in polymyxin-resistant mutants of Escherichia coli. J Biol Chem 279 (2003) 24731-24739. 

T. Morohoshi, T. Maruo, Y. Shirai, J. Kato, T. Ikeda, N. Takiguchi, H. Othake and A. Kuroda (2002). Accumulation of inorganic polyphosphate in phoU mutants of Escherichia coli and Synestocystis sp. strain PCC6803. Appl. Environ. Microbiol., 68, 4107-4110. 

Table I. Phage, Colicin, and Antibiotic Resistance in ton Mutants of Escherichia coli K-12...

Ghosh, P., Meyer, C., Remy, E., Peterson, D., and Preiss, J. 1992. Biosynthesis of bacterial glycogen Cloning, expression and nucleotide sequence of gig C Gene from an allosteric mutant of Escherichia coli B. Arch. Biochem. Biophys. 296,122-128. 

It was found that most of the 2-deoxyribosylic compounds in a trichloroacetic acid extract of the bacteria are present chemically in such a combination that snake-venom treatment is required in order to make them microbiologically active. Furthermore, when the extract was tested without venom pretreatment but in the presence of thymidine, the growth-promoting effect of the 2-deoxyribosylic compounds was 10 times that displayed without thymidine and reached 60% of the activity obtained after venom treatment. The nature of the substances responsible for this effect has not yet been described. The acidic nature of the 2-deoxyri-bosylic compounds was shown by the fact that 98% of the mixture was adsorbed to a Dowex anion exchanger. In the eluted fractions, thymidine 5-phosphate, thymidine 5-pyrophosphate, and thsmiidine 5-triphosphoric acid were identified. From the major 2-deoxyribosylic fraction, thymidine rhamnosyl pyrophosphate (XIX) has been isolated. This substance was also identified in the thymidine-requiring mutant of Escherichia coli 15 T-. 

Small quantities of the 5-amino-4-imidazolecarboxamide nucleotide were also isolated from the culture medium of Escherichia coli grown under sulfonamide bacteriostasis.i i This substance is considered to be an intermediate in purine biosynthesis, both in micro-organisms and in mammalian cells. In sulfonamide-inhibited cells and in the purine-requiring mutant of Escherichia coli, there is a block in the conversion of 5-amino-4-imidazole-carboxamide n-ribonucleotide to inosinic acid. The accumulated nucleotide in the bacterial cell is probably attacked by phosphatases this would explain why the nucleoside is the main metabolite. 

It has been shown that the accumulation of 5-amino-iV-D-ribosyl-4-imidazolecarboxamide in a purine-requiring mutant of Escherichia coli ceases when the bacteria are supplied with an excess of purine. The site of inhibition is, apparently, before the formation of the imidazole ring occurs, but after the formation of the D-ribosyl moiety, since adenine has only a... 

It is reported that a purine-requiring mutant of Escherichia coli accumulated a substance related to 5-amino-iV-D-ribosyl-4-imidazolecarboxamide. Its ultraviolet absorption spectrum and its diazo chromogen spectrum differed from those of the known D-ribosyl derivative. Escherichia coli (strain B-96) converts it to 5-amino-4-imidazolecarboxamide, and it can be utilized by Escherichia coli B. It was suggested that it is an amino-(D-ribosyl)-imidazole. The accumulation of this substance was, however, somewhat surprising, since bacterial extracts of the purine-requiring mutant effected synthesis of 5-amino-4-imidazolecarboxamide from o-ribose 5-phosphate together with adenosine 5-triphosphoric acid and an energy source. 

A mutant of Escherichia coli B, resistant to 2,6-diaminopurine, was found to convert this base to 6-amino-2-methylamino-purine (XXVII) at a rate 60 to 90 % of that of normal cells. The methylated base was isolated from the culture medium, but the organism lacked the ability to incorporate 2,6-diaminopurine or its A-methyl derivative into the nucleotide fraction of the cell. This observation supports previous data which had indicated that resistance to this substance in Lactobacillus casei is due to the loss of an enzyme system responsible for the incorporation of the base into the nucleotide. ... 

Yano, R., Nagai, H., Shiba, K., and Yura, T., 1990, A mutation that enhances synthesis of ct32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli. J. Bacteriol. 172 2124—2130. 

Mao, S. S., Yu, G. X., Chalfoun, D., and Stubbe, J., 1992, Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity, Biochemistry 31 9752n9759. 

Lawrence, C. C., Bennati, M., Obias, H. V., Bar, G., Griffin, R. G., and Stubbe, J., 1999, High-field EPR detection of a disulfide radical anion in the reduction of cytidine 5 -diphosphate by the E441Q R1 mutant of Escherichia coli ribonucleotide reductase. Proc. Natl. Acad. Sci. USA 96 8979ii8984. 

Parkin, S. E., Chen, S. X., Ley, B. A., Mangravite, L., Edmondson, D. E., Huynh, B. H., and Bollinger, J. M., 1998, Electron injection through a specific pathway determines the outcome of oxygen activation at the diiron cluster in the E208Y mutant of Escherichia coli ribonucleotide reductase protein R2. Biochemistry 37 112491130. 

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