DNA-binding proteins in the cytoplasm of vaccinia virus-infected mouse L-cells.
Mouse L cell fibroblasts were infected with vaccinia virus and labeled 2 to 3 h postinfection with [35S]methionine. Labeled proteins were fractionated on native and denatured DNA-cellulose columns and then analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Twenty-four 90,000 to 12,500, were detected. VDP-12A (molecular weight, 29,750) had affinity for denatured but not native DNA, and its synthesis was dependent on viral DNA replication. VDP-20 (molecular weight, 41,000) bound very tightly to native and denatured DNA and was displaced only after boiling the protein-DNA-cellulose matrix in 1% sodium dodecyl sulfate. VDP-8,-11,-12,-13, -and-14 behaved electrophoretically like the polypeptide species previously shown to be present in DNA-protein complexes prepared from infected cells. The molecular weights of VDP-10 (50,000), VDP-11 (36,000), and VDP-8 (67,000) were similar to the polypeptide subunits of polyadenylate polymerase and phosphohydrolase I, enzymes purified from virions which have also been shown to have affinity for DNA.
D003593:Cytoplasm / Q000032:analysis; D004265:DNA Helicases / Q000032:analysis* / Q000096:biosynthesis; D004261:DNA Replication; D004279:DNA, Viral / Q000096:biosynthesis; D007739:L Cells; D008970:Molecular Weight; D009691:Nucleic Acid Denaturation; D010455:Peptides / Q000032:analysis; D014616:Vaccinia virus / Q000032:analysis* / Q000378:metabolism; D014764:Viral Proteins / Q000032:analysis* / Q000096:biosynthesis
D004279:DNA, Viral; D010455:Peptides; D014764:Viral Proteins; D004265:DNA Helicases