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Effect of netropsin on plasmid DNA cleavage by BAL 31 nuclease
Author(s) -
Sakaguchi Reiko,
Joho Ken-ichi,
Shishido Kazuo
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80993-5
Subject(s) - netropsin , nuclease , plasmid , endonuclease , exonuclease , dna , chemistry , microbiology and biotechnology , cleavage (geology) , dna supercoil , biophysics , biochemistry , biology , dna replication , dna polymerase , paleontology , minor groove , fracture (geology)
BAL 31 nuclease is known to possess two sorts of catalytic activities: one is a single‐strand‐specific endonuclease activity that converts negatively supercoiled UNA to the unit‐length linear form, the other being a quasi‐processive exonuclease activity that simultaneously degrades both 3'‐ and 5'‐termini of linear dúplex DNA. Netropsin, a bactericidal and antiviral compound, was found to enhance the former activity but inhibit the latter. Netropsin‐bound supercoiled plasmid DNA had a tendency to be fragmented by BAL 31 into several species of linear DNAs smaller than full‐length size. Size reduction of linear plasmid DNA by BAL 31 was significantly inhibited by netropsin binding.