Myristyl acylation of the tumor necrosis factor alpha precursor on specific lysine residues.
Open accessAbstract
NH2-terminal glycine myristyl acylation is a cotranslational modification that affects both protein localization and function. However, several proteins that lack NH2-terminal glycine residues, including the interleukin 1 (IL-1) precursors, also contain covalently linked myristate. To date, the site(s) of acylation of these proteins has not been determined. During an evaluation of IL-1 acylation, it was observed that [3H]myristate-labeled human monocyte lysates contained a prominent 26-kD myristylated protein, which was identified as the tumor necrosis factor alpha (TNF) precursor protein on the basis of specific immune precipitation. Radioimmunoprecipitates from the supernates of labeled monocytes indicated that the processed or mature 17-kD form of TNF does not contain myristate, suggesting that the site of acylation occurs within the 76-amino acid propiece of the precursor molecule. As the TNF precursor does not contain an NH2-terminal glycine, we hypothesized that myristyl acylation occurs on the N-epsilon-NH2 groups of lysine, of which two are present in the propiece (K19K20). Synthetic peptides were designed to include all seven lysine residues present within the entire 26-kD TNF precursor, and used in an in vitro myristyl acylation assay containing peptide, myristyl-CoA, and monocyte lysate as a source of enzyme. Analysis of reaction products by reverse phase high performance liquid chromatography and gas phase sequencing demonstrated the exclusive myristyl acylation of K19 and K20, consistent with the presence in monocytes of a specific lysyl N-epsilon-NH2-myristyl transferase activity. The acylated lysine residues are located immediately downstream from a hydrophobic, probable membrane-spanning segment of the propiece. Specific myristyl acylation of the TNF propiece may facilitate membrane insertion or anchoring of this critical inflammatory mediator.
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The majority of fatty-acylated proteins have N-glycine myristoylation or S-palmitoylation, while only a few proteins have lysine fatty acylation.
“The majority of these fatty-acylated proteins have been reported to have N-glycine myristoylation or S-palmitoylation, while only a few proteins are reported to have lysine fatty acylation.15,34”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [34]
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- Authors
- Stevenson, F. T., Bursten, S. L., Locksley, R. M., & Lovett, D. H.
- Affiliations
- San Francisco VA Medical Center (US)
- ORCID
- Locksley, R M
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1992-10-01
- Volume
- 176
- Issue
- 4
- Pages
- 1053-1062
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2119375
- OpenAlex
- W2186750753
- Cited by
- 117
- References
- 32
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 5 · 2022: 1 · 2021: 9 · 2020: 5 · 2019: 7 · 2018: 6 · 2017: 6 · 2016: 7 · 2015: 5 · 2014: 6 · 2013: 5 · 2012: 1
- FWCI
- 1.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK AI-26918)
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- lysine acylation, myristate, monocytes, inflammatory mediators
- MeSH terms
- Acylation, Amino Acid Sequence, Animals, Cytosol, Humans, Kinetics, Lysine, Molecular Sequence Data, Monocytes, Myristic Acids, Oligopeptides, Protein Precursors, Protein Processing, Post-Translational, Recombinant Proteins, Tumor Necrosis Factor-alpha, Electrophoresis, Gel, Two-Dimensional, Sequence Homology, Amino Acid, Myristic Acid
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