DNA binding proteins in the cytoplasm of vaccinia virus infected mouse L cells

M. J. Soloski, M. Esteban, J. A. Holowczak

Research output: Contribution to journalArticlepeer-review

Abstract

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 vaccinia DNA-binding polypeptides (VDPs), ranging in molecular weight from 90,000 to 12,500, were detected. VDP-12A (molecular weight, 29,750) had affinity for denatured but not native DNA, and its sythesis 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.

Original languageEnglish (US)
Pages (from-to)263-273
Number of pages11
JournalJournal of virology
Volume25
Issue number1
DOIs
StatePublished - 1978
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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