Appearance of 170,000 dalton phosphoprotein in rat cells transformed by the adenovirus E1A gene.
A highly phosphorylated protein with a molecular size of 170,000 daltons (170K phosphoprotein) was detected in the membrane fraction of HY1 cells transformed by E1A gene but not of the normal rat 3Y1-B cells. Phosphorylation was not dependent on cyclic nucleotides but required divalent metal ion. The major phosphorylated amino acid was phosphoserine. This 170K phosphoprotein was not observed in the membrane fractions of 3Y1 cells transformed by SV40, polyoma, and B77. These results suggest that appearance of the 170K phosphoprotein is related to the function of adenoviral E1A gene.
D000260:Adenoviruses, Human / Q000235:genetics* / Q000502:physiology; D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis; D002472:Cell Transformation, Viral; D005814:Genes, Viral; D008274:Magnesium / Q000494:pharmacology; D008565:Membrane Proteins / Q000032:analysis / Q000096:biosynthesis*; D008970:Molecular Weight; D010750:Phosphoproteins / Q000032:analysis / Q000096:biosynthesis*; D010766:Phosphorylation; D010768:Phosphoserine / Q000032:analysis; D051381:Rats
D008565:Membrane Proteins; D010750:Phosphoproteins; D010768:Phosphoserine; D008274:Magnesium