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

Nature. 1984 Nov 29-Dec 5;312(5993):458-62. 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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular*
  • DNA / metabolism*
  • DNA Replication
  • Escherichia coli / genetics
  • Interleukin-1 / genetics*
  • Interleukin-1 / physiology
  • Leukemia P388 / immunology
  • Mice
  • Plasmids
  • Poly A / genetics
  • RNA / genetics
  • RNA, Messenger / genetics


  • Interleukin-1
  • RNA, Messenger
  • Poly A
  • RNA
  • DNA

Associated data

  • GENBANK/X01450