A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1 beta in Saccharomyces cerevisiae
| Autor: | James A. H. Murray, C. L. Galeotti, Cosima T. Baldari, P. Ghiara, Gianni Cesareni |
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| Předmět: |
Signal peptide
Transcription Genetic Saccharomyces cerevisiae Protein Sorting Signals General Biochemistry Genetics and Molecular Biology Complementary DNA Humans Secretion Molecular Biology Kluyveromyces lactis chemistry.chemical_classification Expression vector General Immunology and Microbiology biology Oligonucleotide General Neuroscience DNA Restriction Enzymes biology.organism_classification Recombinant Proteins Amino acid Molecular Weight chemistry Biochemistry Genes Interleukin-1 Plasmids Research Article |
| Zdroj: | Scopus-Elsevier |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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