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Division of Virology, St. Jude Children's Research Hospital, 332 North Lauderdale, P.O. Box 318, Memphis, Tennessee 38101, U.S.A.
At least 12 virus-induced DNA-binding proteins with mol. wt. ranging from 14 x 103 to 119 x 103 have been isolated from frog virus (FV 3)-infected fathead minnow cells by DNA affinity chromatography. Two enzymic activities, DNA-dependent DNA polymerase and endodeoxyribonuclease, were present in the DNA-binding proteins; these enzymic activities were similar to those induced by FV 3 in infected cells. A single species of DNA-binding protein with a mol. wt. of 36000 had very high affinity for single-stranded DNA, but a low one for double-stranded DNA. Proteins with such characteristic affinity for single-stranded DNA destabilize the DNA helix and are essential for viral DNA replication. Thus, the 36000 mol. wt. DNA-binding protein is a candidate for such a role in FV 3 DNA replication.
Keywords: DNA-binding protein, DNA polymerase, DNase, frog virus 3
Received 26 January 1981;
accepted 5 May 1981.
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