Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation.

@article{Kamps1985MutationON,
  title={Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation.},
  author={Mark P. Kamps and Janice E. Buss and Bartholomew M. Sefton},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1985},
  volume={82 14},
  pages={4625-8}
}
p60src, the transforming protein kinase of Rous sarcoma virus, contains the 14-carbon saturated fatty acid, myristic acid, linked through an amide bond to the alpha-amino group of its NH2-terminal glycine residue. Myristic acid is known to be attached to four other eukaryotic proteins. In each case the fatty acid is also linked through an amide bond to an NH2-terminal glycine. We have used oligonucleotide-directed mutagenesis to examine the amino acid specificity of the enzyme that… CONTINUE READING

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