Abelson murine leukaemia virus protein is phosphorylated in vitro to form phosphotyrosine

Abstract
The Abelson murine leukaemia virus protein (P120) can become phosphorylated in vitro by [γ-32P]ATP. The protein has been purified from cell membranes to the point that in specific conditions virtually all of the incorporated 32P is in P120. The reaction is stimulated by Mn2+ and Mg2+ but not Ca2+ and is very rapid even at 0 °C. The phosphate is linked to P120 at tyrosine, a linkage not previously reported for a phosphorylation reaction. Phosphorylation may be involved in the transforming activity of viruses that cause leukaemia as well as sarcomas.