Characterization of an endonuclease activity associated with Friend-murine leukemia virus.
An endonuclease activity shown to be associated with Friend leukemia virus has been characterized using double-stranded phi X174 DNA as substrate. In the presence of Mg2+, the endonuclease activity was able to convert supercoiled circular DNA duplexes to the relaxed form by introducing single-stranded nicks into the DNA. Most of the nicked DNA duplexes contained only one nick per strand, since unit length DNA was the predominant species obtained when the nicked DNA was analyzed by alkaline sucrose gradient centrifugation. The regions into which the nick could be introduced were evenly distributed around the circular DNA molecule. When Mn2+ was substituted for Mg2+ in the reaction mixture, the number of nicks introduced into circular DNA duplexes by the virus associated endonuclease was greatly increased. In contrast to circular duplexes, linear duplexes and single-stranded DNA functioned poorly as substrates for the virus-associated enzyme. The Friend leukemia virus-associated endonuclease activity is with respect to these characteristics very similar to the endonuclease activity associated with the p32 protein of the avian myeloblastosis virus [1]. The molecular weight of the Friend leukemia virus endonuclease was estimated by gel filtration on a Sephacryl S-200 column to be about 45 000.
D002850:Chromatography, Gel; D004720:Endonucleases / Q000378:metabolism* / Q000494:pharmacology; D005622:Friend murine leukemia virus / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology
D011092:Polyethylene Glycols; D017830:Octoxynol; D004720:Endonucleases; D008274:Magnesium