Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation.
- 1 July 1985
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 82 (14) , 4625-4628
- https://doi.org/10.1073/pnas.82.14.4625
Abstract
P60src, the transforming protein kinase of Rous sarcoma virus, contains the 14-C 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 4 other eukaryotic proteins. In each case the fatty acid is also linked through an amide bond to an NH2-terminal glycine. Oligonucleotide-directed mutagenesis was used to examine the amino acid specificity of the enzyme that myristoylates the NH2 terminus of these proteins. Replacement of the NH2-terminal glycine in p60src with either alanine or glutamic acid prevented myristoylation completely. This indicates that the myristoylating enzyme may have an absolute specificity for glycine. Neither nonmyristoylated mutant src protein induced morphological transformation of infected cells, even though wild-type levels of phosphorylation of cellular proteins on tyrosine were observed in these cells. Since conversion of the NH2-terminal residue from glycine to alanine should have little effect on the conformation of p60src, the inability of this mutant p60src protein to induce morhological transformation suggests that the myristoyl moiety is essential for the transforming activity of the protein.This publication has 29 references indexed in Scilit:
- Stimulation of tyrosine-specific phosphorylation in vitro by insulin-like growth factor INature, 1983
- Nucleotide sequence of rous sarcoma virusCell, 1983
- Myristyl amino-terminal acylation of murine retrovirus proteins: An unusual post-translational protein modificationProceedings of the National Academy of Sciences, 1983
- Identification of the NH2‐terminal blocking group of calcineurin B as myristic acidFEBS Letters, 1982
- n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle.Proceedings of the National Academy of Sciences, 1982
- Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factorNature, 1982
- Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment of DNANucleic Acids Research, 1982
- Evidence that the src gene product of rous sarcoma virus is membrane associatedVirology, 1980
- Localization of the ASV src gene product to the plasma membrane of transformed cells by electron microscopic immunocytochemistryCell, 1979
- The NH2-terminal sequence of the avian oncovirus gag precursor polyprotein (Pr76gag)Virology, 1978