The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG

EMBO J. 1991 Mar;10(3):655-64.

Abstract

The pim-1 gene is frequently found activated by proviral insertion in murine T cell lymphomas. Overexpression of pim-1 in lymphoid cells by transgenesis formally proved its oncogenic potential. The pim-1 cDNA sequence predicts that both murine and human pim-1 encode a 34 kd protein with homology to protein kinases. In this study, we show that the murine pim-1 gene encodes a 44 kd protein in addition to the predicted 34 kd protein. The 44 kd protein is an amino-terminal extension of the 34 kd protein and is synthesized by alternative translation initiation at an upstream CUG codon. Contrary to previous findings by others, we provide evidence that both murine and human pim-1 gene products are protein-serine/threonine kinases. Murine 44 kd and 34 kd pim-1 proteins exhibit comparable in vitro kinase activity and are both mainly cytoplasmic, but they differ in in vivo association state and half-life.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Codon / genetics*
  • Humans
  • Kinetics
  • Mice
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Oligonucleotide Probes
  • Peptide Mapping
  • Protein Biosynthesis*
  • Protein Kinases / genetics*
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-pim-1
  • Proto-Oncogenes*
  • Sequence Homology, Nucleic Acid
  • Transfection

Substances

  • Codon
  • Oligonucleotide Probes
  • Proto-Oncogene Proteins
  • Protein Kinases
  • PIM1 protein, human
  • Pim1 protein, mouse
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-pim-1