Lysine residue 121 in the proposed ATP-binding site of the v-mos protein is required for transformation.
The transforming gene product encoded by Moloney murine sarcoma virus clone 124, p37mos, contains a lysine residue (lysine-121) that is conserved among all members of the protein kinase family. This lysine has been shown to be part of a conserved ATP-binding site in both the catalytic subunit of the cAMP-dependent protein kinase and p60v-src. We wished to determine whether this lysine is required for the transforming activity of p37mos. Two site-specific mutations were therefore constructed, which result in the substitution of an aspartic acid or arginine codon in place of the codon for lysine-121. Both mutations abolished the ability of the mos gene to transform cells. These results show that lysine-121 is required for the ability of p37mos to transform cells and provide evidence for an ATP-binding site in p37mos. Furthermore, these results suggest that the conserved lysine residue is specifically involved in the catalytic activity of protein kinases in general.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D002472:Cell Transformation, Viral; D002522:Chlorocebus aethiops; D008239:Lysine; D008970:Molecular Weight; D008980:Moloney murine sarcoma virus / Q000235:genetics*; D009154:Mutation; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D011494:Protein Kinases / Q000235:genetics*; D009053:Sarcoma Viruses, Murine / Q000235:genetics*; D013329:Structure-Activity Relationship
D009856:Oncogene Proteins, Viral; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D008239:Lysine