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An enzymatic activity in uninfected cells that cleaves the linkage between poliovirion RNA and the 5' terminal protein
Cell (1978)
  • Victor R. Ambros, Massachusetts Institute of Technology
  • Ralf F. Pettersson, Massachusetts Institute of Technology
  • David Baltimore, Massachusetts Institute of Technology
Abstract
The 5' terminal protein (VPg) on poliovirion RNA can be removed by cell-free extracts from a variety of uninfected cells. This soluble enzymatic activity is found in both nuclear and cytoplasmic extracts of heLa cells and is activated by Mg++. The enzyme activity cleaves the tyrosine-phosphate bond that links the protein to the RNA. In a partially purified form it has insufficient nonspecific protease or nuclease activity to account for its action. The existence of this enzyme implies that poliovirus RNA is translated in cell-free extracts in a form that lacks the 5' terminal protein. The role of this enzyme in the uninfected cell is not known.
Disciplines
Publication Date
December, 1978
Citation Information
Victor R. Ambros, Ralf F. Pettersson and David Baltimore. "An enzymatic activity in uninfected cells that cleaves the linkage between poliovirion RNA and the 5' terminal protein" Cell Vol. 15 Iss. 4 (1978)
Available at: http://works.bepress.com/victor_ambros/87/