Effect of netropsin on plasmid DNA cleavage by BAL 31 nuclease

FEBS Letters

Sakaguchi, Reiko¹  Shishido, Kazuo¹  Joho, Ken-ichi¹ 

[1] Laboratory of Natural Products Chemistry, Tokyo Institute of Technology, Nagatsuta, Yokohama, Kanagawa 227, Japan

关键词: Netropsin;    Bactericidal antibiotic;    Antiviral antibiotic;    BAL 31 nuclease;    S1 nuclease;    Plasmid;    DNA structure distortion;   

DOI  :  10.1016/0014-5793(85)80993-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown