The signal peptide of human preproendothelin‐1

FEBS Letters

Benatti, Luca²  Nitti, Gianpaolo²  Valsasina, Barbara²  Fabbrini, Maria Serena¹  Vitale, Alessandro¹ 

[1] Istituto Biosintesi Vegetali, Consiglio Nazionale delle Recerche, via Bassini 15, 20133 Milano, Italy;Biotechnology Dept., Farmitalia Carlo Erba, viale Bezzi 24, 20146, Milano, Italy

关键词: Endothelin biosynthesis;    Endoplasmic reticulum;    Signal peptide;    ER;    endoplasmic reticulum;    ET;    endothelin;   

DOI  :  10.1016/0014-5793(91)80948-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Synthetic mRNAs were produced using either the complete coding sequence of a human preproendothelin-1 cDNA clone or a truncated form in which the portion encoding the first 17 amino acids, representing a putative signal peptide for insertion into the endoplasmic reticulum, was replaced with a methionine codon. The mRNAs were translated in vitro in the presence or in the absence of microsomal membranes. Protection from trypsin digestion demonstrated that the full-length polypeptide, but not the truncated form, could be inserted into the membranes. Sequence analysis revealed that membrane insertion is accompanied by removal of the first 17 amino acids. These results indicate that the first 17 amino acids of human preproendothelin-1 are a functional signal peptide which allows the protein to enter the secretory pathway.

【 授权许可】

Unknown