EcoRI restriction endonuclease map of the composite R plasmid NR1
نویسندگان
چکیده
منابع مشابه
EcoRI restriction endonuclease cleavage site map of bacteriophage P22DNA.
‘l’l~e SWYW EcoKI restriction endonuclease cleavage sites in bacteriophage P%d DNA have been mapped. The cleavage site map of circularly permut.ed P22 linear DNA is a circle. The positions of EcoRI sites in the early region of the P22 genomc were determined by comparing products of EcoRI digestion of maturtx liaear P22 chromosomes with the EcoRI cleavage fragments of DNA of three XimmP22 hybrid...
متن کاملSpecificity of substrate recognition by the EcoRI restriction endonuclease.
The substrate specificity of the EcoRI restriction endonuclease can be varied in vitro by changing the pH and the ionic environment of the reaction. Phosphodiester bond cleavage occurs at a DNA hexanucleotide sequence d(N-G-A-A-T-T-C-N)/d(N-C-T-T-A-A-G-N) when the ionic strength is high, 100 mM Tris-HCl, 50 mM NaCl, 5 mM MgCl2, and the pH is approximately 7.3. Lowering the ionic strength to 25 ...
متن کاملThe EcoRI restriction endonuclease, covalently closed DNA and ethidium bromide.
The reactions of the EcoRI restriction endonuclease on the covalently closed DNA of plasmid pMB9 were studied in the presence of ethidium bromide. At the concentrations of ethidium bromide tested, which covered the range over which the DNA is changed from negatively to positively supercoiled, the dye caused no alteration to the rate at which this enzyme cleaved the covalently closed DNA to yiel...
متن کاملThe kinetic mechanism of EcoRI endonuclease.
Steady-state parameters governing cleavage of pBR322 DNA by EcoRI endonuclease are highly sensitive to ionic environment, with K(m) and k(cat) increasing 1,000-fold and 15-fold, respectively, when ionic strength is increased from 0.059 to 0.23 M. By contrast, pre-steady-state analysis has shown that recognition, as well as first and second strand cleavage events that occur once the enzyme has a...
متن کاملPhysical map and strand polarity of specific fragments of adenovirus-associated virus DNA produced by endonuclease R-EcoRI.
Cleavage of adenovirus-associated virus type 2 (AAV2) DNA linear duplex monomers with the restriction endonuclease R-EcoRI yielded three fragments, A, B, and C, having approximate mol wt of 1.6 X 10(6), 1.1 X 10(6), and 1.3 X 10(5), respectively. Radioactive labeling the 5' termini of AAV DNA before cleavage with R-EcoRI showed that A and B were terminal fragments and C was internal. Separation...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1976
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.127.1.619-636.1976