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The signal peptide of human preproendothelin‐1
Author(s) -
Fabbrini Maria Serena,
Valsasina Barbara,
Nitti Gianpaolo,
Benatti Luca,
Vitale Alessandro
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80948-3
Subject(s) - signal peptide , endoplasmic reticulum , signal peptidase , amino acid , biology , complementary dna , biochemistry , peptide sequence , methionine , peptide , microbiology and biotechnology , gene
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.