The myristylation signal of p60v-src functionally complements the N-terminal fps-specific region of P130gag-fps.
The P130gag-fps protein-tyrosine kinase of Fujinami sarcoma virus contains an N-terminal fps-specific domain (Nfps) that is important for oncogenicity. The N-terminal 14 amino acids of p60v-src, which direct myristylation and membrane association, can replace the gag-Nfps sequences of P130gag-fps (residues 1 to 635), producing a highly transforming src-fps polypeptide. Conversely, gag-Nfps can restore modest transforming activity to a nonmyristylated v-src polypeptide. These results emphasize the modular construction of protein-tyrosine kinases and indicate that Nfps, possibly in conjunction with gag, functions in the subcellular localization of P130gag-fps.
Brooks-Wilson
A R
AR
Division of Molecular and Developmental Biology, Mount Sinai Hospital Research Institute, Toronto, Ontario, Canada.
Ball
E
E
Pawson
T
T
D000595:Amino Acid Sequence; D001483:Base Sequence; D002461:Cell Line, Transformed; D004247:DNA / Q000235:genetics; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D009227:Myristic Acids / Q000378:metabolism; D009856:Oncogene Proteins, Viral / Q000235:genetics*; D011505:Protein-Tyrosine Kinases / Q000235:genetics*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism
D009227:Myristic Acids; D009856:Oncogene Proteins, Viral; D011994:Recombinant Proteins; D004247:DNA; D011505:Protein-Tyrosine Kinases