A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1 beta in Saccharomyces cerevisiae.

C. Baldari, J. A. Murray, P. Ghiara, G. Cesareni, C. L. Galeotti

Research output: Contribution to journalArticlepeer-review

Abstract

Killer strains of Kluyveromyces lactis secrete a toxin which presumably is processed during secretion from a larger precursor. Analysis of the sequence of the K. lactis killer toxin gene predicts that the first 16 amino acids at the amino terminus of the protein should represent its leader peptide. We have tested the capability of this leader peptide to direct secretion of a protein fused to it by inserting a synthetic oligonucleotide identical to the sequence of the putative leader peptide into a yeast expression vector. Subsequently, the cDNA coding for the secreted active portion of the human interleukin 1 beta (IL-1 beta) was fused to the leader peptide sequence of the killer toxin. This construction in Saccharomyces cerevisiae is capable of directing synthesis and secretion of correctly processed IL-1 beta into the culture medium.

Original languageEnglish
Pages (from-to)229-234
Number of pages6
JournalEMBO Journal
Volume6
Issue number1
Publication statusPublished - Jan 1987

ASJC Scopus subject areas

  • Cell Biology
  • Genetics

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