COMPETENCE FOR GENETIC TRANSFORMATION IN ACINETOBACTER CALCOACETICUS NCIB8250
FEMS Microbiology LettersPublished 1 February 1980Open access
Eric Fredolin Ahlquist, C. A. Fewson, DA. RITCHIE, J. PODMORE, V. Rowell
Citations20
SJR quartileQ3
SJR score0.60
SNIP0.59
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Abstract
E.F. Ahlquist, C.A. Fewson, D.A. Ritchie, J. Podmore, V. Rowell; Competence for genetic transformation in Acinetobacter calcoaceticus NCIB8250, FEMS Microb
Keywords
Biochemistry, Genetics and Molecular BiologyEngineering
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The availability of a strain of Acinetobacter competent for transformation has made it possible to demonstrate the genetic relatedness of a large variety of gram-negative, oxidase- negative, nonmotile, and aerobic coccobacilli originally classified into eleven different genera.
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The chapter describes that the enzymology of recombination in transformation and transfection is a difficult problem to solve, as there are indications of alternative enzymatic pathways for recombination, so that mutants blocked in one pathway may not necessarily show loss of ability to be transformed or transfected.
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Adenosine 3':5'-cyclic monophosphate added to exponentially growing cells of Hemophilus influenzae strain Rd increases competence for transformation 100- to 10,000-fold and Cyclic AMP added to near-stationary or stationary cells does not increase competence over the high level normally found in the early stationary phase.
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Auxotrophs of Acinetobacter calcoaceticus blocked in each reaction of the synthetic pathway from chorismic acid to tryptophan were obtained after N-methyl-N'-nitro-N-nitrosoguanidine mutagenesis, and one novel class was found to be blocked in both anthranilate and p-aminobenzoate synthesis.
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Deoxyribonucleic acid from 250 strains of aerobic, nonfermentative, gram-negative coccobacilli and rods were tested for the ability to transform a stable competent auxotroph of Acinetobacter to prototrophy by using the method established by Juni.
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The production of mutant forms of the enzyme from Acinetobacter lwofi (a Gram-negative aerobe) by transformation is reported, which might contribute to an understanding of the molecular requirements for the production of a tetrameric, rather than a dimeric, enzyme.
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