An N-terminal peptide from p60src can direct myristylation and plasma membrane localization when fused to heterologous proteins
- PMID: 3920530
- DOI: 10.1038/314374a0
An N-terminal peptide from p60src can direct myristylation and plasma membrane localization when fused to heterologous proteins
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. Myristic acid is bound in an amide linkage to glycine 2 of p60src. 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 transformation. 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), or to the chimpanzee alpha-globin gene. 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.
Similar articles
-
Processing of p60v-src to its myristylated membrane-bound form.Mol Cell Biol. 1985 Oct;5(10):2781-8. doi: 10.1128/mcb.5.10.2781-2788.1985. Mol Cell Biol. 1985. PMID: 3016513 Free PMC article.
-
Fine structural mapping of a critical NH2-terminal region of p60src.Proc Natl Acad Sci U S A. 1985 Mar;82(6):1623-7. doi: 10.1073/pnas.82.6.1623. Proc Natl Acad Sci U S A. 1985. PMID: 2984663 Free PMC article.
-
Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein.Science. 1985 Jan 25;227(4685):427-9. doi: 10.1126/science.3917576. Science. 1985. PMID: 3917576
-
Transformation by p60src with altered N-terminal sequences.Princess Takamatsu Symp. 1986;17:233-40. Princess Takamatsu Symp. 1986. PMID: 2843496 Review.
-
Function, location, and regulation of the src protein-tyrosine kinase.Princess Takamatsu Symp. 1989;20:63-70. Princess Takamatsu Symp. 1989. PMID: 2484925 Review.
Cited by
-
Structure and expression of c-fgr protooncogene mRNA in Epstein-Barr virus converted cell lines.Br J Cancer. 1988 Dec;58(6):704-9. doi: 10.1038/bjc.1988.294. Br J Cancer. 1988. PMID: 2852026 Free PMC article.
-
Myristylation site in Pr65gag is essential for virus particle formation by Moloney murine leukemia virus.Proc Natl Acad Sci U S A. 1986 Oct;83(19):7246-50. doi: 10.1073/pnas.83.19.7246. Proc Natl Acad Sci U S A. 1986. PMID: 3489936 Free PMC article.
-
Nucleotide sequence of the src gene of the Schmidt-Ruppin strain of Rous sarcoma virus type E.Nucleic Acids Res. 1989 Feb 11;17(3):1252. doi: 10.1093/nar/17.3.1252. Nucleic Acids Res. 1989. PMID: 2537953 Free PMC article. No abstract available.
-
Isolation and oncogenic potential of a novel human src-like gene.Mol Cell Biol. 1986 Dec;6(12):4195-201. doi: 10.1128/mcb.6.12.4195-4201.1986. Mol Cell Biol. 1986. PMID: 3099169 Free PMC article.
-
Inhibitory monoclonal antibody against a (myristylated) small-molecular-weight antigen from Plasmodium falciparum associated with the parasitophorous vacuole membrane.Infect Immun. 1988 Apr;56(4):903-9. doi: 10.1128/iai.56.4.903-909.1988. Infect Immun. 1988. PMID: 3278984 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous
