Cloning and expression of murine interleukin-1 cDNA in Escherichia coli

• Published in: Nature (London) Vol. 312; no. 5993; pp. 458 - 462
• Main Authors: Lomedico, Peter T, Gubler, Ueli, Hellmann, Christopher P, Dukovich, Mitchell, Giri, Judith G, Pan, Yu-Ching E, Collier, Kenneth, Semionow, Raina, Chua, Anne O, Mizel, Steven B
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 01-01-1984
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Biotechnology; cDNA; Cell physiology; Cloning, Molecular; DNA - metabolism; DNA Replication; Escherichia coli; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Health. Pharmaceutical industry; Hormonal regulation; Industrial applications and implications. Economical aspects; interleukin 1; Interleukin-1 - genetics; Interleukin-1 - physiology; Leukemia P388 - immunology; Mice; Molecular and cellular biology; Other active biomolecules; Plasmids; Poly A - genetics; Production of active biomolecules; RNA - genetics; RNA, Messenger - genetics; transformation; Escherichia coli; Interleukin; Rodentia; Peptide hormone; Primary structure; Gene expression; Biological activity; Vertebrata; Mammalia; Complementary DNA; Mouse; Bacteria; Biosynthesis precursor; Molecular cloning; Escherichieae; Enterobacteriaceae
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/312458a0

Interleukin-1 (IL-1), a peptide hormone produced by activated macrophages, possesses the ability to modulate the proliferation, maturation and functional activation of a broad spectrum of cell types and may play a major role in the initiation and amplification of immune and inflammatory responses through its action on these diverse cell populations. IL-1 exhibits microheterogeneity in terms of its relative molecular mass (Mr, 13,000-19,000) and charge properties, and although murine IL-1 has been purified and some of its basic structure-function relationships have been elucidated, it has proved difficult to prepare sufficient amounts of IL-1 for direct and detailed sequence and structural studies. Here we report the cloning, sequence analysis and expression of murine IL-1 cDNA in Escherichia coli. The IL-1 cDNA codes for a polypeptide precursor of 270 amino acids. Biologically active IL-1 was produced in E. coli by expressing the carboxy-terminal 156 amino acids of the IL-1 precursor.