myristic acid/саркома

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Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein.

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Myristic acid, a minor component of cellular fatty acids, has been shown previously to be covalently bound to most molecules of p60src, the transforming protein of Rous sarcoma virus. We have now determined at what time during the life cycle of p60src, and where within the cell, this lipid becomes

Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog.

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The lipid bound to p60src, the transforming protein of Rous sarcoma virus, has been identified by gas and thin-layer chromatography as the 14-carbon saturated fatty acid, myristic acid. The protein can be labeled biosynthetically with either [3H]myristic acid or [3H]palmitic acid. Incorporation of

Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation.

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Mutagenesis of glycine 2 of p60src, the transforming protein of Rous sarcoma virus (RSV), yields a protein that is neither myristylated nor bound to cellular membranes. Although these mutant viruses retain full tyrosine protein kinase activity, they are transformation-defective. We examined in

Myristylation of Rous sarcoma virus Gag protein does not prevent replication in avian cells.

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Rous sarcoma virus is an example of a replication-competent retrovirus whose Gag protein is not modified with myristic acid. The purpose of the experiments described in this report was to determine whether the addition of this 14-carbon fatty acid would interfere with the replication of Rous sarcoma

Avian sarcoma virus gag-fps and gag-yes transforming proteins are not myristylated or palmitylated.

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The transforming proteins of several avian sarcoma viruses were examined for evidence of covalently attached fatty acids. While the product of the viral src gene could be readily labeled biosynthetically with [3H]myristic acid, the gag-onc transforming proteins of Fujinami sarcoma virus, PRCII,

Creation and expression of myristylated forms of Rous sarcoma virus gag protein in mammalian cells.

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Rous sarcoma virus (RSV), a member of the avian sarcoma and leukosis family of retroviruses, has long been known to be capable of infecting and transforming mammalian cells; however, such transformed cells do not release virus particles. The RSV gag product (Pr76gag) produced in these cells is not

Myristic acid is incorporated into the two acylatable domains of the functional glycoprotein CD9 in ester, but not in amide bonds.

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CD9 is a signal-initiating glycoprotein of uncertain membrane insertion which contains more than one locus of acylation and is distinguished by being the major acylatable platelet protein. The N-terminus of CD9 is blocked to Edman degradation. We investigated whether [3H]myristic acid could be

Functional analysis of protein N-myristoylation: metabolic labeling studies using three oxygen-substituted analogs of myristic acid and cultured mammalian cells provide evidence for protein-sequence-specific incorporation and analog-specific redistribution.

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Covalent attachment of myristic acid (C14:0) to the NH2-terminal glycine residue of a number of cellular, viral, and oncogene-encoded proteins is essential for full expression of their biological function. Substitution of oxygen for methylene groups in this fatty acid does not produce a significant

In vivo modification of retroviral gag gene-encoded polyproteins by myristic acid.

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It has recently been shown by mass spectral analysis (Henderson et al., Proc. Natl. Acad. Sci. U.S.A. 80:339-343, 1983) that the p15gag protein of murine leukemia viruses contains a novel post-translational modification, an amino-terminal myristyl (tetradecanoyl) amide. In this report we show that

RNA dimerization defect in a Rous sarcoma virus matrix mutant.

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The retrovirus matrix (MA) sequence of the Gag polyprotein has been shown to contain functions required for membrane targeting and binding during particle assembly and budding. Additional functions for MA have been proposed based on the existence of MA mutants in Rous sarcoma virus (RSV), murine

The cytoskeletal protein vinculin is acylated by myristic acid.

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In non-muscle cells the mechanism by which microfilament bundles interact with the plasma membrane is unclear. Vinculin, a 130 kDa protein found in adhesion plaques, has been postulated to have a role as a membrane anchor for microfilaments and we have investigated the biochemistry of this molecule

The absence of myristic acid decreases membrane binding of p60src but does not affect tyrosine protein kinase activity.

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We have constructed two point mutants of Rous sarcoma virus in which the amino-terminal glycine residue of the transforming protein, p60src, was changed to an alanine or a glutamic acid residue. Both mutant proteins failed to become myristylated and, more importantly, no longer transformed cells.

Characterization of N-myristoyl transferase inhibitors and their effect on HIV release.

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Acylation of virus proteins is an important covalent modification which has been shown, in many cases, to be necessary for their normal function. Furthermore, it has been shown that cerulenin, an inhibitor of this process, inhibits formation of vesicular stomatitis virus and Rous sarcoma virus in

Direct identification of palmitic acid as the lipid attached to p21ras.

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p21v-H-ras, the transforming protein of Harvey murine sarcoma virus, contains a covalently attached lipid. Using thin-layer chromatography, we identified the acyl group as the 16-carbon saturated fatty acid palmitic acid. No myristic acid was detected in fatty acids released from in vivo-labeled

In vitro synthesis of pp60v-src: myristylation in a cell-free system.

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Covalent attachment of myristic acid to pp60v-src, the transforming protein of Rous sarcoma virus, was studied in a cell-free system. Using a synthetic peptide containing the first 11 amino acids of the mature pp60v-src polypeptide sequence as a substrate, we probed lysates from a variety of cells

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