A Trans-acting Protein Kinase Identified in Cells Transformed by Abelson Murine Leukemia Virus

  1. O. N. Witte,
  2. L. Sun,
  3. N. Rosenberg*, and
  4. D. Baltimore
  1. Department of Biology and Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139; *Cancer Research Center and Department of Pathology, Tufts University School of Medicine, Boston, Massachusetts 02111

This extract was created in the absence of an abstract.

Excerpt

Abelson murine leukemia virus (Ab-MuLV) is a transformation-defective retrovirus derived from the Moloney murine leukemia virus (M-MuLV). The basic biology, genomic structure, mRNA species, protein translation products, and serological characterization of Ab-MuLV are reviewed elsewhere (Baltimore et al., this volume). The prototype Ab-MuLV strain is known to encode a single major polyprotein with a molecular weight (m.w.) of 120,000 (P120) and an amino-terminal region (∼30,000 m.w.) derived from retained sequences of the M-MuLV genome. A car-boxyterminal region (∼90,000 m.w.) encoded from the Ab-MuLV unique sequences contains distinctive antigenic determinants (Witte et al. 1978, 1979).

Recently, strain variants have been isolated that differ in the size of the Ab-MuLV polyprotein encoded (Rosenberg et al., this volume). All current isolates (90,000–160,000 m.w.) retain a common amino-terminal M-MuLV-derived region and a region encoding an Ab-MuLV-specific antigen; therefore, they probably differ at their carboxyl termini. All the isolates tested were phosphoproteins (Witte et al...

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