Skip to main content
Log in

Demonstration of multiple forms of bovine brain myristoyl CoA: protein N-myristoyl transferase

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

Four distinct N-myristoyl transferase (NMT) activity peaks, designated I, II, III, and IV, were separated from the cytosolic fraction of bovine brain by DEAE-Sepharose column chromatography. Peaks I, II, III and IV were characterised biochemically with respect to substrate specificity; with cAMP-dependent protein kinase and pp60src derived peptides, and by their apparent molecular mass. The apparent molecular mass of peaks I, II, III and IV were 190 kDa, 224 kDa, 390 kDa and 76 kDa, respectively. These results indicate that bovine brain contains multiple forms of NMT.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

NMT:

Myristoyl-CoA : protein N-myristoyl Transferase

EGTA:

Ethylene Glycol bis(β-aminoethyl ether) N,N,N′,N′,-tetraacetic acid

References

  1. Towler DA, Gordon JI, Adams SP, Glaser L: The biology and enzymology of eukaryotic protein acylation. Ann Rev Biochem 57: 69–99, 1988

    Google Scholar 

  2. Grand RAJ: Acylation of viral and eukaryotic proteins. Biochem J 258: 625–638, 1989

    Google Scholar 

  3. Deichaite I, Casson LP, Ling HP, Resh MD: In vitro synthesis of pp60src. Myristoylation in a cell-free system. Mol Cell Biol 8: 4295–4301, 1988

    Google Scholar 

  4. Carr SA, Biemann K, Shozo S, Parmelee DC, Titani K: nTetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle, Proc Natl Acad Sci USA 79: 6128–6131, 1982

    Google Scholar 

  5. Aitken A, Cohen P, Santikarn S, Williams DH, Calder AG, Smith A, Klee CB: Identification of the NH2-terminal blocking group of calcineurin B as myristic acid. FEBS Lett 150: 314–318, 1982

    Google Scholar 

  6. Buss JE, Kamps MP, Sefton BM: Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membranebound forms of the protein, Mol Cell Biol 4: 2697–2704, 1984

    Google Scholar 

  7. Buss JE, Mumby SM, Casey PJ, Gilman AG, Sefton BM: Myristoylated a subunits of guanine nucleotide-binding regulatory proteins. Proc Natl Acad Sci USA 84: 7493–7497, 1987

    Google Scholar 

  8. Schultz AM, Tsai S-C, Kung H-F, Oroszlan S, Moss J, Vaughan M: Hydroxylamine-stable covalent linkage of myristic acid in G00, a guanine nucleotide-binding protein from bovine brain, Biochem Biophys Res Commun 146: 1234–1239, 1987

    Google Scholar 

  9. Rein A, McClure MR, Rice NR, Luftig RB, Schultz AM: Myristoylation site in Pr65gag is essential for virus particle formation by Moloney leukemia virus, Proc Natl Acad Sci USA 83: 7246–7250, 1986

    Google Scholar 

  10. Towler DW, Glaser L: Protein fatty acid acylation: Enzymatic synthesis of a N-myristoylglycyl peptide, Proc Natl Acad Sci USA 83: 2812–2816, 1986

    Google Scholar 

  11. Heuckeroth RO, Towler DW, Adams SP, Glaser L, Gordon JI: 11-(Ethylthio)undecanoic acid, A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferases. J Biol Chem 263: 2127–2133, 1988

    Google Scholar 

  12. Glover CJ, Goddard C, Felsted RL: N-Myristoylation of p60src. Identification of a myristoyl-CoA: glycylpeptide-N-myristoyl transferase in rat tissue, Biochem J 250: 485–491, 1988

    Google Scholar 

  13. Towler DW, Adams SP, Eubanks SH, Towery DS, Jackson-Machelski E, Glaser L, Gordon JI: Myristoyl CoA: protein N-myristoyl transferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities. J Biol Chem 263: 1784–1790, 1988

    Google Scholar 

  14. Paige LA, Chafin DR, Cassady JM, Geahlen RL: Detection of myristoyl CoA: protein N-myristoyl transferase activity by ionexchange chromatography, Anal Biochem 181: 254–258, 1989

    Google Scholar 

  15. McIlhinney RAJ, McGlone K: Characterisation of a myristoyl-CoA: glycylpeptide N-myristoyl transferase activity in rat brain: Subcellular and regional distribution. J Neurochem 54: 110–117, 1990

    Google Scholar 

  16. Towler DW, Adams SP, Eubanks SH, Towery DS, Adams SP, Glaser L: Amino-terminal processing by N-myristoylation. Substrate specificity of N-myristoyl transferase. J Biol Chem 262: 1030–1036, 1987

    Google Scholar 

  17. Towler DW, Adams SP, Eubanks SH, Towery DS, Jackson-Machelski E, Glaser L, Gordon JI: Purification and characterisation of yeast myristoyl-CoA: protein N-myristoyl transferase. Proc Natl Acad Sci USA 84: 2708–2712, 1987

    Google Scholar 

  18. King MJ, Sharma RK: N-myristoyl transferase assay using phosphocellulose paper binding. Anal Biochem 199: 149–153, 1991

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

King, M.J., Sharma, R.K. Demonstration of multiple forms of bovine brain myristoyl CoA: protein N-myristoyl transferase. Mol Cell Biochem 113, 77–81 (1992). https://doi.org/10.1007/BF00230888

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00230888

Key words

Navigation