A NOVEL LEADER PEPTIDE WHICH ALLOWS EFFICIENT SECRETION OF A FRAGMENT OF HUMAN INTERLEUKIN 1-BETA IN SACCHAROMYCES-CEREVISIAE

被引：168

作者：

BALDARI, C ^{[1
]}

MURRAY, JAH ^{[1
]}

GHIARA, P ^{[1
]}

CESARENI, G ^{[1
]}

GALEOTTI, CL ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB, D-6900 HEIDELBERG, GERMANY

来源：

EMBO JOURNAL | 1987年 / 6卷 / 01期

关键词：

D O I：

10.1002/j.1460-2075.1987.tb04743.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：229 / 234

页数：6

共 34 条

[1] NUCLEOTIDE-SEQUENCE OF HUMAN MONOCYTE INTERLEUKIN-1 PRECURSOR CDNA [J].