Hypersensitive mung bean nuclease cleavage sites in Plasmodium knowlesi DNA |
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Authors: | P Szafrański G N Godson |
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Affiliation: | Polish Academy of Sciences, Institute of Biochemistry and Biophysics, Warsaw. |
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Abstract: | Nucleotide sequences of Plasmodium knowlesi DNA that are cleaved by mung bean nuclease (Mbn) at low enzyme concentration (0.2 units enzyme per micrograms DNA) are listed. They are tandemly repeated purine/pyrimidine (RpY) stretches of DNA with (ApT) dimers predominating. Most cut sites are within almost 100% RpY tracts. The enzyme cleaves at many points within the RpY stretch and usually hydrolyzes the 5'-ApT-3' linkage. These alternating RpY target sites are flanked by homopurine and homopyrimidine stretches. At least one Mbn target site lies next to an in vivo transcribed region. |
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