An N-terminal peptide from p60src can direct myristylation and plasma membrane localization when fused to heterologous proteins

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Abstract
The src gene product, p60src, of Rous sarcoma virus (RSV) is a tyrosine-specific protein kinase which is associated with the plasma membrane of infected cells (for review, see ref. 1). Myristic acid is bound in an amide linkage to glycine 2 of p60src (refs 2–6). Of the N-terminal 30 kilodaltons of p60src only amino acids 1–14 are required for myristylation, and myristylation of p60src may be required for its membrane association, and for cell transformation4,7. To test the hypothesis that the first 14 amino acids of p60src contain a recognition sequence for myristylation, we have fused the DNA sequence coding for these amino acids to either the fps gene of the F36 derivative of Fujinami sarcoma virus (FSV)8,9, or to the chimpanzee α-globin gene10. We report here that although the fusion proteins were myristylated, the parental proteins were not, and unlike the non-myristylated F36 p91fps which was not bound to the plasma membrane, the myristylated fusion protein was bound, like p60src. We conclude that the first 14 amino acids of p60src contain a sequence which is sufficient for myristylation, and which may direct proteins to the plasma membrane.