A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1 beta in Saccharomyces cerevisiae.
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.
D004262:DNA Restriction Enzymes; D005796:Genes; D006801:Humans; D007375:Interleukin-1 / Q000032:analysis / Q000235:genetics*; D008970:Molecular Weight; D010957:Plasmids; D021382:Protein Sorting Signals / Q000378:metabolism*; D011994:Recombinant Proteins / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D014158:Transcription, Genetic
D007375:Interleukin-1; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D004262:DNA Restriction Enzymes